1ho8
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ho8' size='340' side='right'caption='[[1ho8]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='1ho8' size='340' side='right'caption='[[1ho8]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ho8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ho8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HO8 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ho8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho8 OCA], [https://pdbe.org/1ho8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho8 ProSAT]</span></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=1ho8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho8 OCA], [https://pdbe.org/1ho8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/VATH_YEAST VATH_YEAST] Vacuolar ATPases regulate the organelle acidity. This subunit is essential for activity, but not assembly, of the enzyme complex. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ho8 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ho8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | In contrast to the F-type ATPases, which use a proton gradient to generate ATP, the V-type enzymes use ATP to actively transport protons into organelles and extracellular compartments. We describe here the structure of the H-subunit (also called Vma13p) of the yeast enzyme. This is the first structure of any component of a V-type ATPase. The H-subunit is not required for assembly but plays an essential regulatory role. Despite the lack of any apparent sequence homology the structure contains five motifs similar to the so-called HEAT or armadillo repeats seen in the importins. A groove, which is occupied in the importins by the peptide that targets proteins for import into the nucleus, is occupied here by the 10 amino-terminal residues of subunit H itself. The structural similarity suggests how subunit H may interact with the ATPase itself or with other proteins. A cleft between the amino- and carboxyl-terminal domains also suggests another possible site of interaction with other factors. | ||
- | |||
- | Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae.,Sagermann M, Stevens TH, Matthews BW Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7134-9. PMID:11416198<ref>PMID:11416198</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1ho8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[ATPase 3D structures|ATPase 3D structures]] | *[[ATPase 3D structures|ATPase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: | + | [[Category: Matthews BW]] |
- | [[Category: | + | [[Category: Sagermann M]] |
- | [[Category: | + | [[Category: Stevens TH]] |
- | + |
Current revision
CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE
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