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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gordon-Smith DJ,Carbajo RJ,Yang JC,Videler H,Runswick MJ,Walker JE,Neuhaus D

doi

10.1006/jmbi.2001.4570

keywords:

subject

Has Abstract

pub_date

2001-04-27 00:00:00

pages

325-39

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(01)94570-X

journal_volume

308

pub_type

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