1ho8

<StructureSection load='1ho8' size='340' side='right' caption='[[1ho8]], [[Resolution|resolution]] 2.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ho8]] 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=1HO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HO8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ho8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho8 OCA], [http://pdbe.org/1ho8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ho8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ho8 PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ho/1ho8_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1ho8" style="background-color:#fffaf0;"></div>

*[[ATPase|ATPase]]

[[Category: Atcc 18824]]

[[Category: Matthews, B W]]

[[Category: Sagermann, M]]

[[Category: Stevens, T H]]

[[Category: Heat repeat]]

[[Category: Hydrolase]]