1hf9

From Proteopedia

Revision as of 14:26, 20 November 2007

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

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