1PXY

Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin

Summary for 1PXY

• Entry DOI: 10.2210/pdb1pxy/pdb
• Descriptor: fimbrin-like protein (2 entities in total)
• Functional Keywords: calponin homology, f-actin-binding domain (abd), f-actin-crosslinking, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, structural protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 115095.29

Authors

Klein, M.G.,Shi, W.,Tseng, Y.,Wirtz, D.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-07-07, release date: 2004-06-22, Last modification date: 2023-08-16)

Primary citation

Klein, M.G.,Shi, W.,Ramagopal, U.,Tseng, Y.,Wirtz, D.,Kovar, D.R.,Staiger, C.J.,Almo, S.C.
Structure of the actin crosslinking core of fimbrin.
Structure, 12:999-1013, 2004

PubMed 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.

PubMed: 15274920
DOI: 10.1016/j.str.2004.04.010

Experimental method

X-RAY DIFFRACTION (2.4 Å)