Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase

D Gordon-Smith, R Carbajo, J Yang, H Videler, M Runswick, J Walker, D Neuhaus (2001) Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase J Mol Biol (IF: 4.5) 308(2) 325-39

Abstract

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.Copyright 2001 Academic Press.

Links

http://www.ncbi.nlm.nih.gov/pubmed/11327770
http://dx.doi.org/10.1006/jmbi.2001.4570

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