1ho8: Difference between revisions

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[[Image:1ho8.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE==
|PDB= 1ho8 |SIZE=350|CAPTION= <scene name='initialview01'>1ho8</scene>, resolution 2.95&Aring;
<StructureSection load='1ho8' size='340' side='right'caption='[[1ho8]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<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>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
|GENE=  
<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>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ho/1ho8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE'''
==See Also==
 
*[[ATPase 3D structures|ATPase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1HO8 is a [[Single protein]] structure of 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=1HO8 OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11416198 11416198]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Matthews BW]]
[[Category: Matthews, B W.]]
[[Category: Sagermann M]]
[[Category: Sagermann, M.]]
[[Category: Stevens TH]]
[[Category: Stevens, T H.]]
[[Category: SO4]]
[[Category: heat repeat]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:40 2008''

Latest revision as of 10:29, 7 February 2024

CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAECRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE

Structural highlights

1ho8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.95Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VATH_YEAST Vacuolar ATPases regulate the organelle acidity. This subunit is essential for activity, but not assembly, of the enzyme complex.

Evolutionary Conservation

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

See Also

1ho8, resolution 2.95Å

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