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1qqv
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SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN
Overview
A growing family of F-actin-bundling proteins harbors a modular F-actin-binding headpiece domain at the C terminus. Headpiece provides one of the two F-actin-binding sites essential for filament bundling. Here, we report the first structure of a functional headpiece domain. The NMR structure of chicken villin headpiece (HP67) reveals two subdomains that share a tightly packed hydrophobic core. The N-terminal subdomain contains bends, turns, and a four-residue alpha-helix as well as a buried histidine residue that imparts a pH-dependent folding. The C-terminal subdomain is composed of three alpha-helices and its folding is pH-independent. Two residues previously implicated in F-actin-binding form a buried salt-bridge between the N and C-terminal subdomains. The rest of the identified actin-binding residues are solvent-exposed and map onto a unique F-actin-binding surface.
About this Structure
1QQV is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
NMR structure of an F-actin-binding "headpiece" motif from villin., Vardar D, Buckley DA, Frank BS, McKnight CJ, J Mol Biol. 1999 Dec 17;294(5):1299-310. PMID:10600386
Page seeded by OCA on Thu Mar 20 13:41:29 2008
