1QQV

SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN

Summary for 1QQV

• Entry DOI: 10.2210/pdb1qqv/pdb
• NMR Information: BMRB: 4428
• Descriptor: VILLIN HEADPIECE DOMAIN (1 entity in total)
• Functional Keywords: f-actin binding domain, salt-bridge, structural protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Cytoplasm, cytoskeleton: P02640
• Total number of polymer chains: 1
• Total formula weight: 7611.66

Authors

Vardar, D.,Buckley, D.A.,Frank, B.S.,McKnight, C.J. (deposition date: 1999-06-08, release date: 1999-12-29, Last modification date: 2024-05-22)

Primary citation

Vardar, D.,Buckley, D.A.,Frank, B.S.,McKnight, C.J.
NMR structure of an F-actin-binding "headpiece" motif from villin.
J.Mol.Biol., 294:1299-1310, 1999

PubMed Abstract: 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.

PubMed: 10600386
DOI: 10.1006/jmbi.1999.3321

Experimental method

SOLUTION NMR