1hf9
From Proteopedia
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| - | [[Image:1hf9.png|left|200px]] | ||
| - | + | ==C-Terminal Coiled-Coil Domain from Bovine IF1== | |
| + | <StructureSection load='1hf9' size='340' side='right'caption='[[1hf9]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hf9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HF9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf9 OCA], [https://pdbe.org/1hf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hf9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface. | ||
| - | + | Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.,Gordon-Smith DJ, Carbajo RJ, Yang JC, Videler H, Runswick MJ, Walker JE, Neuhaus D J Mol Biol. 2001 Apr 27;308(2):325-39. PMID:11327770<ref>PMID:11327770</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 1hf9" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Carbajo | + | [[Category: Large Structures]] |
| - | [[Category: Gordon-Smith | + | [[Category: Carbajo RJ]] |
| - | [[Category: Neuhaus | + | [[Category: Gordon-Smith DJ]] |
| - | [[Category: Runswick | + | [[Category: Neuhaus D]] |
| - | [[Category: Videler | + | [[Category: Runswick MJ]] |
| - | [[Category: Walker | + | [[Category: Videler H]] |
| - | [[Category: Yang | + | [[Category: Walker JE]] |
| - | + | [[Category: Yang J-C]] | |
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Current revision
C-Terminal Coiled-Coil Domain from Bovine IF1
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