View source for 2rpw


==Structure of a peptide derived from H+-V-ATPase subunit a==
<StructureSection load='2rpw' size='340' side='right'caption='[[2rpw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rpw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RPW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpw OCA], [https://pdbe.org/2rpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rpw RCSB], [https://www.ebi.ac.uk/pdbsum/2rpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rpw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_YEAST] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:11278748, PubMed:1491220, PubMed:8798414). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:1491220). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:8798414).<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 3D structure of a peptide derived from the putative transmembrane segment 7 (TM7) of subunit a from H(+)-V-ATPase from Saccharomyces cerevisiae has been determined by solution state NMR in SDS. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738, as was previously suggested based on NMR studies of a similar peptide in DMSO. The pKa of both histidine residues that are important for proton transport was measured in water and in SDS. The differences that are found demonstrate that the histidine residues interact with the SDS polar heads. In detergent, circular dichroism data indicate that the secondary structure of the peptide depends on the pH and the type of detergent used. Using solid-state NMR, it is shown that the peptide is immobile in phospholipid bilayers, which means that it is probably not a single transmembrane helix in these samples. The environment is important for the structure of TM7, so in subunit a it is probably held in place by the other transmembrane helices of this subunit.

Structural properties of a peptide derived from H+ -V-ATPase subunit a.,Vermeer LS, Reat V, Hemminga MA, Milon A Biochim Biophys Acta. 2009 May;1788(5):1204-12. Epub 2009 Feb 26. PMID:19249284<ref>PMID:19249284</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rpw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Hemminga MA]]
[[Category: Milon A]]
[[Category: Reat V]]
[[Category: Vermeer LS]]