1hf9

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf9 OCA], [http://www.ebi.ac.uk/pdbsum/1hf9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hf9 RCSB]</span>
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'''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1'''
'''C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1'''
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[[Category: Walker, J E.]]
[[Category: Walker, J E.]]
[[Category: Yang, J C.]]
[[Category: Yang, J C.]]
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[[Category: f1 atpase inhibitor]]
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[[Category: F1 atpase inhibitor]]
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[[Category: mitochondrion]]
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[[Category: Mitochondrion]]
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[[Category: transit peptide]]
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[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:47:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:03:53 2008''
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Revision as of 15:47, 2 May 2008

Template:STRUCTURE 1hf9

C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1


Overview

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.

About this Structure

1HF9 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 18:47:22 2008

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