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1u7l

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Revision as of 19:11, 10 September 2015

Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

Structural highlights

1u7l is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	VMA5 (ATCC 18824)
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[VATC_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system of eukaryotic cells. It provides most of the energy required for transport systems that utilize the proton-motive force that is generated by ATP hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to those of F-ATPase and the nonhomologous subunits determine the unique features of V-ATPase. We determined the crystal structure of V-ATPase subunit C (Vma5p), which does not show any homology with F-ATPase subunits, at 1.75 A resolution. The structural features suggest that subunit C functions as a flexible stator that holds together the catalytic and membrane sectors of the enzyme. A second crystal form that was solved at 2.9 A resolution supports the flexible nature of subunit C. These structures provide a framework for exploring the unique mechanistic features of V-ATPases.

Crystal structure of yeast V-ATPase subunit C reveals its stator function.,Drory O, Frolow F, Nelson N EMBO Rep. 2004 Dec;5(12):1148-52. PMID:15540116^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Parra KJ, Keenan KL, Kane PM. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J Biol Chem. 2000 Jul 14;275(28):21761-7. PMID:10781598 doi:http://dx.doi.org/10.1074/jbc.M002305200
↑ Drory O, Frolow F, Nelson N. Crystal structure of yeast V-ATPase subunit C reveals its stator function. EMBO Rep. 2004 Dec;5(12):1148-52. PMID:15540116

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u7l"

@@ Line 2: / Line 2: @@
 <StructureSection load='1u7l' size='340' side='right' caption='[[1u7l]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u7l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U7L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u7l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U7L FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VMA5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VMA5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u7l RCSB], [http://www.ebi.ac.uk/pdbsum/1u7l PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7l OCA], [http://pdbe.org/1u7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u7l RCSB], [http://www.ebi.ac.uk/pdbsum/1u7l PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1u7l" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Atcc 18824]]
 [[Category: Drory, O]]
 [[Category: Frolow, F]]

1u7l

From Proteopedia

Revision as of 19:11, 10 September 2015

Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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