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J Mol Biol. 2001 Apr 27;308(2):325-39.

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

Author information

1
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.

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.

PMID:
11327770
DOI:
10.1006/jmbi.2001.4570
[Indexed for MEDLINE]

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