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Topic: Transmembrane ATPase

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 Transmembrane ATPase   (Site not responding. Last check: 2007-10-20)
Transmembrane ATPases are integral membrane proteins that use energy from the hydrolysis of adenosine triphosphate (ATP) to transport ions and other solutes between the solutions on either side of a biological membrane and against a solute's natural direction of flow.
Transmembrane ATPases harness the chemical potential energy of ATP, because they perform work: they transport solutes in a direction opposite to their thermodynamically preferred direction of movement—that is, from the side of the membrane where they are in low concentration to the side where they are in high concentration.
The ATP synthetase (or ATP synthase) of mitochondria and chloroplasts is an anabolic enzyme that harnesses the energy of a transmembrane proton gradient as an energy source for adding an inorganic phosphate group to a molecule of adenosine diphosphate (ADP) to form a molecule of adenosine triphosphate (ATP).
publicliterature.org /en/wikipedia/t/tr/transmembrane_atpase.html   (322 words)

 ATPase Information Center - calcium atpase
ATPases are a class of enzymes that atpase inhibitor catalyze the decomposition of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and na k atpase function a free phosphate ion.
Transmembrane ATPases import many of the metabolites necessary for cell metabolism and export toxins, wastes, and solutes that sodium potassium atpase pump can hinder cellular processes.
Transmembrane ATPases harness the chemical potential energy of ATP, because they perform mechanical work: they transport solutes in a direction opposite to their thermodynamically preferred direction of movement—that is, from the side of the membrane where they are in low concentration to chloroplast atpase the side where they are atpase immobilization in high concentration.
www.scipeeps.com /Sci-Biochemistry_Topics_A/ATPase.html   (416 words)

An electrogenic transmembrane ATPase common to all cellular life alternately known as the Na
The electrical and concentration gradient established by the sodium-potasium ATPase supports not only the cell resting potential but theaction potentials of nerves and muscles.
Export of sodium from the cell provides the driving force for several facilitated transporters, which import glucose, amino acids and other nutrients into the cell.
www.ebroadcast.com.au /lookup/encyclopedia/na/NaKATPase.html   (242 words)

 Transport Across Cell Membranes   (Site not responding. Last check: 2007-10-20)
Transmembrane proteins create a water-filled pore through which ions and some small hydrophilic molecules can pass by diffusion.
Transmembrane proteins, called transporters, use the energy of ATP to force ions or small molecules through the membrane against their concentration gradient.
The crucial roles of the Na ATPase are reflected in the fact that almost one-third of all the energy generated by the mitochondria in animal cells is used just to run this pump.
home.comcast.net /~john.kimball1/BiologyPages/D/Diffusion.html   (2794 words)

Similarly, deletions or insertions in transmembrane helices were adjusted to allow them to span the bilayer, as in the structural model, and in some cases were adjusted to align aromatic residues at the membrane interface.
All transmembrane helices are clustered together to form transmembrane domain M which is contained within the hydrophobic lipid bilayer.
Transmembrane domains are underlined and the conserved aspartate characteristic of all P-type ATPases is marked with an arrow.
www.bmb.psu.edu /faculty/halleck/structure/Structure.htm   (1842 words)

 Proton pump
For example, the translocation of protons by cytochrome c oxidase is powered by reducing equivalents provided by reduced cytochrome c.
In the plasma membrane proton ATPase and in the ATPase proton pumps of other cellular membranes, ATP itself powers this transport.
ATP synthase of mitochondria and the CF ATP synthetase of chloroplasts, in contrast, usually conduct protons from high to low concentration across the membrane while drawing energy from this flow to synthesize ATP.
www.ebroadcast.com.au /lookup/encyclopedia/pr/Proton_pump.html   (143 words)

 Interaction of D-600 with the transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase -- Ortega et al. 279 (1): ...
ATPase activity in LSR was determined by a colorimetric technique, based on the reaction between P
The transition temperatures at various concentrations of D-600 calculated from the denaturation profile of the Ca -ATPase component B are given in Table 2.
the ATPase or disrupts the lipid bilayer neighboring the transmembrane
ajpcell.physiology.org /cgi/content/full/279/1/C166   (4235 words)

 MacLennan Lab Research Calcium ATPase
The key features include a transmembrane domain made up of 10 transmembrane alpha helices, a stalk sector made up of helical extensions of transmembrane helices, and cytopasmic beta-strand, phosphorylation and nucleotide binding domains attached to the stalk domain at a distance of 60 Å from the transmembrane domain.
We are using site-directed disulfide mapping of transmembrane helices to determine their orientation relative to each other at a few Å resolution, we are analysing the significance of a calcium binding motif that we defined recently and we are attempting to purify cytoplasmic domains for eventual crystallization and structural determination.
Vilsen, B., Andersen, J.P., Clarke, D.M. and MacLennan, D.H. Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2(+)-ATPase of sarcoplasmic reticulum.
www.utoronto.ca /maclennan/rint1.htm   (1712 words)

 Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane ...
transmembrane ERAD substrates are retained in the ER.
A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator.
Riordan, J.R. Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein.
www.jcb.org /cgi/content/full/160/2/157   (4537 words)

 Bjørn Panella Pedersen's homepage | P-type ATPases
This means the diversification of the P-type ATPase family occurred prior to the separation of eubacteria, archaea and eucaryota, stressing the significance of this protein family for cell survival.
One contains all known Cu /Ag ATPases and one is involved in transport of the transition/heavy metals Zn /Cd /Pb /Co The ATPases with type IB classification all have 8 putative transmembrane helices, 1-6 metal binding motifs N-terminal and a highly conserved CP[C/H] motif in the sixth transmembrane helix.
Using standard ATPase assays this enzyme was shown to be active at high temperatures and this activity was stimulated by Cu or Ag ions (Mandal et al.
www.bioxray.dk /~bjopp/p-type_atpases.php   (3083 words)

 Na+/K+-ATPase - Wikipedia, the free encyclopedia
It features superscript or subscript characters that are substituted or omitted because of technical limitations.
It is found in the plasma membrane of virtually every human cell and is common to all cellular life.
The electrical and concentration gradient established by the sodium-potassium ATPase supports not only the cell resting potential but the action potentials of nerves and muscles.
en.wikipedia.org /wiki/NaKATPase   (654 words)

 Energy Conversion in F<sub>0</sub>-ATPase
unit utilizes a transmembrane electrochemical potential (proton motive force), converting it into the mechanical energy of the stalk rotation.
We seek to identify and explore the chain of the elementary chemical (proton transfer) and mechanical (domain motion) events involved in the process of converting the electrochemical energy of the transmembrane proton gradient into the mechanical energy of the c subunit oligomer rotation.
The ultimate challenge is to understand how proton translocation across the membrane, which includes a sequence of local (~10A) proton transfer events, drives the rotation of the large (~70A) c subunit oligomer coupled to the central stalk.
www.ks.uiuc.edu /Research/f0atpase   (286 words)

 PANTHER - Family Information
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane.
ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.
The H(+)-transporting two-sector ATPase (EC: is a component of the cytoplasmic membrane of eubacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts.
www.pantherdb.org /panther/family.do?clsAccession=PTHR11410   (491 words)

 Entrez PubMed
Sodium dodecyl sulfate solubilization of hydrophobic peptides, electrophoresis, and microsequencing of transblotted electrophoretic bands revealed that the fluorescent NCD4 label resides in a segment of tryptic fragment A1, intervening between Glu231 and Glu309.
This segment includes two transmembrane helices, and does not include the domain involved in the phosphoryl transfer reaction during catalytic activity.
On the other hand, the fluorescence emission of intrinsic tryptophan residues clustered within or near the transmembrane region of the ATPase, is distinctly affected by NCD4 label specifically bound to the ATPase, and NCD4 label nonspecifically bound to the sarcoplasmic reticulum membrane.
www.umbi.umd.edu /~collins/myoinformatics/pubmeds/071-full.htm   (373 words)

Abstract: Ion-translocating ATPases are key cellular enzymes that utilize the free energy of ATP hydrolysis to generate transmembrane electrochemical ion gradients that in turn fuel a variety of vital biological processes including absorption, secretion, transmembrane signalling, nerve impulse transmission, excitation/contraction coupling, and growth and differentiation.
A major family of ion-translocating ATPase with about 80 members from all parts of the evolutionary tree is the P-type ATPase family, so named for the participation of a high energy aspartyl- phosphoryl-enzyme intermediate in their catalytic cycle.
An elucidation Of the molecular mechanism by which the P-type ATPases transduce the chemical energy of ATP hydrolysis into transmembrane ion gradients is a primary goal remaining in the transport field.
www.med.unc.edu /wrkunits/1dean/research/Scarborough356.html   (416 words)

 Molecular Evaluation of the Plasma Membrane Proton Pump from Aspergillus fumigatus -- Burghoorn et al. 46 (3): 615 -- ...
Ten putative hydrophobic transmembrane segments are shaded, consensus intron sequences are underlined, and the three extra insertion regions are boxed.
The highly conserved sequence TGES and transmembrane segments TM3, TM4, TM9, and TM10 are shaded.
Transmembrane segments TM1 to TM10 are designated, and the Aspergillus insertion regions are shaded.
aac.asm.org /cgi/content/full/46/3/615   (3954 words)

 Homology modeling of the cation binding sites of Na+K+-ATPase -- Ogawa and Toyoshima 99 (25): 15977 -- Proceedings of ...
Variable residues (shown in fl) among Na -ATPase of different origins are exposed to lipids, whereas Q930 (M8) and E961 (M9) orient toward the center of the transmembrane region.
The transmembrane helices (cylinders) are viewed from the cytoplasmic side.
to be common to all of the P-type ATPases.
www.pnas.org /cgi/content/full/99/25/15977   (4021 words)

Consistent with their substrate specificities and direction of transport, i.e., metal efflux from the cytoplasm, they confer metal tolerance to archaea and bacteria, while in higher eukaryotes they are responsible for metal micronutrient absorption, distribution and clearance.
P1B-type ATPases contain 6-8 transmembrane fragments carrying signature sequences in segments flanking the large ATP binding cytoplasmic loop.
Mutagenesis of the invariant transmembrane Cys in H6, Asn and Tyr in H7 and Met and Ser in H8 of the Archaeoglobus fulgidus Cu+-ATPase has revealed that their side chains likely coordinate the metals during transport and constitute a central unique component of these enzymes [4].
users.wpi.edu /~jalab/res.html   (953 words)

 Ca2+ATPase Home Page
The P-type ATPases use the chemical energy from ATP to transport ions across the membrane against a concentration gradient.
The Ca ATPase (EC that carries out this pumping is a representative member of the P-type ATPase enzymes group.
ATPase, the Ca ATPase from skeletal muscle sarcoplasmic reticulum is structurally and functionally the best-studied member known today.
www.bioinformaticscourses.com /ISB/sp2003/1EUL   (508 words)

 The nongastric H+-K+-ATPases: molecular and functional properties -- Jaisser and Beggah 276 (6): 812 -- AJP - Renal ...
P-ATPases are membrane ATPases involved in ion transport (33, 37, 52).
Role of the transmembrane and extracytoplasmic domain of beta subunits in subunit assembly, intracellular transport, and functional expression of Na,K-pumps.
Embryonic expression of the putative gamma subunit of the sodium pump is required for acquisition of fluid transport capacity during mouse blastocyst development.
ajprenal.physiology.org /cgi/content/full/276/6/F812   (5859 words)

 Entrez-PubMed   (Site not responding. Last check: 2007-10-20)
Do transmembrane segments in proteolyzed sarcoplasmic reticulum Ca(2+)-ATPase retain their functional Ca2+ binding properties after removal of cytoplasmic fragments by proteinase K? Juul B, Turc H, Durand ML, Gomez de Gracia A, Denoroy L, Moller JV, Champeil P, le Maire M. Department of Biophysics, University of Aarhus, Denmark.
C-terminal membranous peptides containing the putative transmembrane segments M7 to M10 accumulated after prolonged proteolysis, as well as large water-soluble fragments containing most of the phosphorylation and ATP-binding domain.
We conclude that in the absence of Ca2+, the complex of membrane-spanning segments in proteolyzed Ca(2+)-ATPase is labile, probably because of relatively free movement or rearrangement of individual segments.
www.biophys.au.dk /References/jvm/jvm1.htm   (220 words)

 CiteULike: The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys(693) and Asp(714) in ...   (Site not responding. Last check: 2007-10-20)
Lys(693) and Asp(714) in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity.
Two cysteine-containing motifs, CAAC near the N-terminus and CPC in transmembrane helix 6, are involved in binding of the translocated metal.
ZntA carrying the change D714M has strong metal-independent ATPase activity and is very weakly phosphorylated both by ATP and P(i).
www.citeulike.org /user/Terkko/article/790826   (531 words)

 Locating Phospholamban in Co-Crystals with Ca2+-ATPase by Cryoelectron Microscopy -- Young et al. 81 (2): 884 -- ...
ATPase activity was used to assess the functional interaction between PLB and Ca -ATPase before crystallization (Table 1).
The atomic coordinates in (d) and (f) are color-coded according to domain: A (yellow), N (green), and P (magenta) transmembrane, stalk, and lumenal domains are white.
Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy.
www.biophysj.org /cgi/content/full/81/2/884   (5081 words)

 ATP synthase   (Site not responding. Last check: 2007-10-20)
This ATPase activity was further associated with the creation of ATP by yet another long series of experiments in many laboratories.
In the 1960s through the 1970s, Paul Boyer developed his binding change, or flip-flop, mechanism, which postulated that ATP synthesis is coupled with a conformational change in the ATP synthase generated by rotation of the gamma subunit.
Large enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria which do not have an electron transport chain, and hydrolyze ATP to make a proton gradient, which they use for flagella and transport of nutrients into the cell.
atp-synthase.iqnaut.net   (565 words)

 Tufts University, Program in Cellular & Molecular Physiology
Zhang,Z., Inoue,T., Forgac,M. and Wilkens,S. Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immunoelectron microscopy.
Kawasaki-Nishi,S., Nishi,T. and Forgac,M. 2003 Interacting helical surfaces of the transmembrane segments of subunits a and c’ of the yeast V-ATPase defined by disilfide-mediated cross-linking.
Leng,X.H., Nishi,T. and Forgac,M. Transmembrane topography of the 100 kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase.
www.tufts.edu /sackler/physiology/faculty/forgac/publications.html   (606 words)

 Predicted location and limited accessibility of protein kinase A phosphorylation site on Na-K-ATPase -- Sweadner and ...
transmembrane spans (2, 3, 24, 29, 37, 40, 44,
The transmembrane domain is shown in aqua, and bound Ca ions can be seen as pale spheres.
B: the transmembrane domain alone is shown, as viewed from the cytoplasm with the other domains cut away.
ajpcell.physiology.org /cgi/content/full/280/4/C1017   (5921 words)

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