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CRYSTAL STRUCTURE OF THE ACTIN-CROSSLINKING CORE OF SCHIZOSACCHAROMYCES POMBE FIMBRIN
Structural highlights
FunctionFIMB_SCHPO Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Plays a role in cytokinesis. Plays important roles in mating and in spore formation.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFilamentous 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. Structure of the actin crosslinking core of fimbrin.,Klein MG, Shi W, Ramagopal U, Tseng Y, Wirtz D, Kovar DR, Staiger CJ, Almo SC Structure. 2004 Jun;12(6):999-1013. PMID:15274920[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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