PDBsum entry 2vik

Actin-binding protein

PDB id: 2vik

Contents

Protein chain

126 a.a. *

* Residue conservation analysis

PDB id:

2vik

Name:

Actin-binding protein

Title:

Refined structure of the actin-severing domain villin 14t, determined by solution nmr, minimized average structure

Structure:

Villin 14t. Chain: a. Fragment: residues 1 - 126. Synonym: villin domain 1, villin segment 1. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Cell_line: bl21. Organ: intestine. Cell: epithelial cells. Gene: t7. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

1 models

Authors:

M.A.Markus,P.Matsudaira,G.Wagner

Key ref:

M.A.Markus et al. (1997). Refined structure of villin 14T and a detailed comparison with other actin-severing domains. Protein Sci, 6, 1197-1209. PubMed id: 9194180 DOI: 10.1002/pro.5560060608

Date:

16-Jan-97 Release date: 01-Apr-97

Protein chain

P02640  (VILI_CHICK) -  Villin-1 from Gallus gallus

Seq: 826 a.a.

Struc: 126 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/pro.5560060608

Protein Sci 6:1197-1209 (1997)

PubMed id: 9194180

Refined structure of villin 14T and a detailed comparison with other actin-severing domains.

M.A.Markus, P.Matsudaira, G.Wagner.

ABSTRACT

Villin 14T is the amino terminal actin monomer binding domain from the actin-severing and bundling protein villin. Its structure has been determined in solution using heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy (Markus MA, Nakayama T, Matsudaira P, Wagner G. 1994. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Protein Science 3:70-81). An additional nuclear Overhauser effect (NOE) spectroscopy data set, acquired using improved gradient techniques, and further detailed analysis of existing data sets, produced an additional 601 NOE restraints for structure calculations. The overall fold does not change significantly with the additional NOE restraints but the definition of the structure is improved, as judged by smaller deviations among an ensemble of calculated structures that adequately satisfy the NMR restraints. Some of the side chains, especially those in the hydrophobic core of the domain, are much more defined. This improvement in the detail of the solution structure of villin 14T makes it interesting to compare the structure with the crystal structure of gelsolin segment 1, which shares 58% sequence identity with villin 14T, in an effort to gain insight into villin 14T's weaker affinity for actin monomers. Villin 14T has smaller side chains at several positions that make hydrophobic contacts with actin in the context of gelsolin segment 1. The structure is also compared with the structure of the related actin-severing domain, severin domain 2.

Selected figure(s)

Figure 5.
Fig. 5. Pairwisecomparisonofdomainsfrom the actin severing family. : V~llin 14T (blue) and gelsolii segment 1 (red). B: Vilin 14T andseverindomain 2 (violet).Thestructures are rotatedcomparedtoFig.1 so thathelix a2, which is the enter for hydrophobicinteractionswithactin, is in front.The structures are presented as tereopairs of ribbondagrams,generatedwithQuanta

Figure 7.
ig. 7. of the surfaces for interaction with actin monomers on villin 14T (A) and gelsolin segment 1 (B) with the corresponding surface on severin domain 2 (C). Electrostatic potentials have been mapped onto the surfaces, with more negative regions shown in red nd more positive regions shown in The asterisks denote the approximate position of lk79 ilh 14T and Ileio3 in gelsolin segment 1, the enterfor hydrophobic interactions with actin monomers. This igure was generated with GRASP (Nicholls et al., 1991).

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1997, 6, 1197-1209) copyright 1997.

Figures were selected by an automated process.