1v9m

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[[Image:1v9m.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus==
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|PDB= 1v9m |SIZE=350|CAPTION= <scene name='initialview01'>1v9m</scene>, resolution 1.85&Aring;
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<StructureSection load='1v9m' size='340' side='right'caption='[[1v9m]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1v9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V9M FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9m OCA], [https://pdbe.org/1v9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v9m RCSB], [https://www.ebi.ac.uk/pdbsum/1v9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v9m ProSAT], [https://www.topsan.org/Proteins/RSGI/1v9m TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1v9m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft.
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'''Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus'''
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Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.,Numoto N, Kita A, Miki K Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125<ref>PMID:15103125</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1v9m" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft.
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1V9M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9M OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103125 15103125]
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[[Category: H(+)-transporting two-sector ATPase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Kita, A.]]
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[[Category: Kita A]]
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[[Category: Miki, K.]]
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[[Category: Miki K]]
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[[Category: Numoto, N.]]
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[[Category: Numoto N]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: GOL]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomic]]
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[[Category: the c subunit]]
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[[Category: thermus thermophilus]]
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[[Category: v-type atpase]]
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[[Category: vov1-atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:42 2008''
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Current revision

Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus

PDB ID 1v9m

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