PDBsum entry: 1rt8

Structural protein

PDB id: 1rt8

Contents

Protein chain

467 a.a. *

Ligands

SO4 ×5

Waters ×104

* Residue conservation analysis

PDB id:

1rt8

Name:

Structural protein

Title:

Crystal structure of the actin-crosslinking core of schizosaccharomyces pombe fimbrin

Structure:

Fimbrin. Chain: a. Fragment: actin-crosslinking core, amino acids 108-614. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.00Å R-factor: 0.237 R-free: 0.270

Authors:

M.G.Klein,W.Shi,U.Ramagopal,Y.Tseng,D.Wirtz,D.R.Kovar, C.J.Staiger,S.C.Almo

Key ref:

M.G.Klein et al. (2004). Structure of the actin crosslinking core of fimbrin. Structure, 12, 999. PubMed id: 15274920 DOI: 10.1016/j.str.2004.04.010

Date:

10-Dec-03 Release date: 22-Jun-04

Protein chain

O59945  (FIMB_SCHPO) -  Fimbrin

Seq: 614 a.a.

Struc: 467 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: actin binding (1 term)

DOI no: 10.1016/j.str.2004.04.010

Structure 12:999 (2004)

PubMed id: 15274920

Structure of the actin crosslinking core of fimbrin.

M.G.Klein, W.Shi, U.Ramagopal, Y.Tseng, D.Wirtz, D.R.Kovar, C.J.Staiger, S.C.Almo.

ABSTRACT

Filamentous actin is organized into bundles and orthogonal networks by the fimbrin/alpha-actinin superfamily of F-actin crosslinking proteins. The crystal structure of the Arabidopsis thaliana and Schizosaccharomyces pombe fimbrin cores provides the first description of a functional F-actin crosslinking protein and highlights the compact and distinctly asymmetric organization of the fimbrin molecule, in which the two actin binding domains present distinct surfaces to solvent. The mapping of functionally important residues onto the structure affords new insights into the binding process and provides additional constraints which must be accommodated by models for F-actin binding and crosslinking. Most strikingly, this work provides unique insight into the mechanistic features of conditional-lethal mutants and their extragenic suppressors, which highlight conformational and dynamic properties required for fimbrin function. These results underscore the power of jointly considering structural and genetic suppressor data for obtaining unexpected and biologically relevant mechanistic information.

Selected figure(s)

Figure 3.
Figure 3. Structure of Schizosaccharomyces Fimbrin Core(A) Stereoview of the a carbon backbone of S.p. core.(B) Superposition of A.t. and S.p. fimbrin structures highlighting the identical compact antiparallel packing arrangement between ABD1 and ABD2 and the variability in the placement of CH2 within ABD1. The sequence of the S.p. core is 42% identical to the A.t. core (alignment spans 503 residues; Figure 1). The similarities in the structures of two fimbrin orthologs and the high degree of conservation at the CH1/CH4 interface suggest that this compact organization is a general and biologically relevant feature of the entire fimbrin family.

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 999-0) copyright 2004.

Figure was selected by an automated process.