2rpw
From Proteopedia
(Difference between revisions)
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| - | + | ==Structure of a peptide derived from H+-V-ATPase subunit a== | |
| - | === | + | <StructureSection load='2rpw' size='340' side='right' caption='[[2rpw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2rpw]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RPW FirstGlance]. <br> | ||
| + | </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=2rpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rpw RCSB], [http://www.ebi.ac.uk/pdbsum/2rpw PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[V-ATPase|V-ATPase]] | *[[V-ATPase|V-ATPase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Hemminga, M A | + | </StructureSection> |
| - | [[Category: Milon, A | + | [[Category: Hemminga, M A]] |
| - | [[Category: Reat, V | + | [[Category: Milon, A]] |
| - | [[Category: Vermeer, L S | + | [[Category: Reat, V]] |
| + | [[Category: Vermeer, L S]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
[[Category: Hydrogen ion transport]] | [[Category: Hydrogen ion transport]] | ||
Revision as of 13:51, 17 December 2014
Structure of a peptide derived from H+-V-ATPase subunit a
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