1PXY

Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin

1PXY の概要

• エントリーDOI: 10.2210/pdb1pxy/pdb
• 分子名称: fimbrin-like protein (2 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115095.29

構造登録者

Klein, M.G.,Shi, W.,Tseng, Y.,Wirtz, D.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2003-07-07, 公開日: 2004-06-22, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)