1rt8
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(New page: 200px<br /><applet load="1rt8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rt8, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 23:44, 20 November 2007
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CRYSTAL STRUCTURE OF THE ACTIN-CROSSLINKING CORE OF SCHIZOSACCHAROMYCES POMBE FIMBRIN
Overview
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.
About this Structure
1RT8 is a Single protein structure of sequence from Schizosaccharomyces pombe with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
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
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