1pxy
From Proteopedia
(New page: 200px<br /><applet load="1pxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pxy, resolution 2.4Å" /> '''Crystal structure of ...) |
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| - | [[Image:1pxy.gif|left|200px]]<br /><applet load="1pxy" size=" | + | [[Image:1pxy.gif|left|200px]]<br /><applet load="1pxy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pxy, resolution 2.4Å" /> | caption="1pxy, resolution 2.4Å" /> | ||
'''Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin'''<br /> | '''Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Filamentous actin is organized into bundles and orthogonal networks by the | + | 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== | ==About this Structure== | ||
| - | 1PXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http:// | + | 1PXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Klein, M | + | [[Category: Klein, M G.]] |
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Shi, W.]] | [[Category: Shi, W.]] | ||
[[Category: Tseng, Y.]] | [[Category: Tseng, Y.]] | ||
| Line 29: | Line 29: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:43 2008'' |
Revision as of 12:33, 21 February 2008
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Crystal structure of the actin-crosslinking core of Arabidopsis 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
1PXY is a Single protein structure of sequence from Arabidopsis thaliana. 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
Page seeded by OCA on Thu Feb 21 14:33:43 2008
Categories: Arabidopsis thaliana | Single protein | Almo, S C. | Burley, S K. | Klein, M G. | NYSGXRC, New York Structural GenomiX Research Consortium. | Shi, W. | Tseng, Y. | Wirtz, D. | Calponin homology | F-actin-binding domain (abd) | F-actin-crosslinking | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
