1YU5

Crystal Structure of the Headpiece Domain of Chicken Villin

Summary for 1YU5

• Entry DOI: 10.2210/pdb1yu5/pdb
• Related: 1qqv 1qzp 1ujs 1vii
• Descriptor: Villin (2 entities in total)
• Functional Keywords: alpha helix, 3-10 helix, structural protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Cytoplasm, cytoskeleton: P02640
• Total number of polymer chains: 1
• Total formula weight: 7611.66

Authors

Meng, J.,Vardar, D.,Wang, Y.,Guo, H.C.,Head, J.F.,McKnight, C.J. (deposition date: 2005-02-11, release date: 2005-09-06, Last modification date: 2024-04-03)

Primary citation

Meng, J.,Vardar, D.,Wang, Y.,Guo, H.C.,Head, J.F.,McKnight, C.J.
High-resolution crystal structures of villin headpiece and mutants with reduced f-actin binding activity.
Biochemistry, 44:11963-11973, 2005

PubMed Abstract: Villin-type headpiece domains are approximately 70 amino acid modular motifs found at the C terminus of a variety of actin cytoskeleton-associated proteins. The headpiece domain of villin, a protein found in the actin bundles of the brush border epithelium, is of interest both as a compact F-actin binding domain and as a model folded protein. We have determined the high-resolution crystal structures of chicken villin headpiece (HP67) at 1.4 A resolution as well as two mutants, R37A and W64Y, at 1.45 and 1.5 A resolution, respectively. Replacement of R37 causes a 5-fold reduction in F-actin binding affinity in sedimentation assays. Replacement of W64 results in a much more drastic reduction in F-actin binding affinity without significant changes in headpiece structure or stability. The detailed comparison of these crystal structures with each other and to our previously determined NMR structures of HP67 and the 35-residue autonomously folding subdomain in villin headpiece, HP35, provides the details of the headpiece fold and further defines the F-actin binding site of villin-type headpiece domains.

PubMed: 16142894
DOI: 10.1021/bi050850x

Experimental method

X-RAY DIFFRACTION (1.4 Å)