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1gmj
From Proteopedia
(Difference between revisions)
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<StructureSection load='1gmj' size='340' side='right'caption='[[1gmj]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1gmj' size='340' side='right'caption='[[1gmj]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1gmj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1gmj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMJ 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]] 2.2Å</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=1gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmj OCA], [https://pdbe.org/1gmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmj RCSB], [https://www.ebi.ac.uk/pdbsum/1gmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmj 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=1gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmj OCA], [https://pdbe.org/1gmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmj RCSB], [https://www.ebi.ac.uk/pdbsum/1gmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ATIF1_BOVIN ATIF1_BOVIN] Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase.<ref>PMID:7397110</ref> <ref>PMID:10831597</ref> <ref>PMID:18687699</ref> <ref>PMID:21192948</ref> <ref>PMID:12923572</ref> <ref>PMID:17895376</ref> | |
== 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=1gmj 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=1gmj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase. | ||
| - | |||
| - | The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase.,Cabezon E, Runswick MJ, Leslie AG, Walker JE EMBO J. 2001 Dec 17;20(24):6990-6. PMID:11742976<ref>PMID:11742976</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1gmj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cabezon | + | [[Category: Cabezon E]] |
| - | [[Category: Leslie | + | [[Category: Leslie AGW]] |
| - | [[Category: Runswick | + | [[Category: Runswick MJ]] |
| - | [[Category: Walker | + | [[Category: Walker JE]] |
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Revision as of 11:22, 27 March 2024
The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase
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