Heterogeneity and dynamics in villin headpiece crystal structures.
The villin headpiece domain (HP67) is the C-terminal F-actin-binding motif that confers F-actin-bundling activity to villin, a component of the actin bundles that support the brush-border microvilli. It has been investigated extensively by both experimental and theoretical measurements. Our laboratory, for example, has determined both its NMR and its crystal structures. This study presents the structures of HP67 and its pH-stabilized mutant (H41Y) in a different crystal form and space group. For both constructs, two molecules are found in each asymmetric unit in the new space group P6(1). While one of the two structures (Mol A) is structurally similar to our previously determined structure (Mol X), the other (Mol B) has significant deviations, especially in the N-terminal subdomain, where lattice contacts do not appear to contribute to the difference. In addition, the structurally most different crystal structure, Mol B, is actually closer to the averaged NMR structure. Harmonic motions, as suggested by the B-factor profiles, differ between these crystal structures; crystal structures from the same space group share a similar pattern. Thus, heterogeneity and dynamics are observed in different crystal structures of the same protein even for a protein as small as villin headpiece.
Meng
Jianmin
J
Boston University School of Medicine, USA.
McKnight
Christopher James
CJ
D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000235:genetics*; D002645:Chickens; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009038:Motion; D020125:Mutation, Missense; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D002352:Carrier Proteins