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| | <StructureSection load='1pxy' size='340' side='right'caption='[[1pxy]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1pxy' size='340' side='right'caption='[[1pxy]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pxy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PXY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pxy]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXY FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxy OCA], [http://pdbe.org/1pxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pxy RCSB], [http://www.ebi.ac.uk/pdbsum/1pxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxy ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1pxy TOPSAN]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxy OCA], [https://pdbe.org/1pxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxy RCSB], [https://www.ebi.ac.uk/pdbsum/1pxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxy ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1pxy TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FIMB1_ARATH FIMB1_ARATH]] Cross-links actin filaments (F-actin) in a calcium independent manner. Stabilizes and prevents F-actin depolymerization mediated by profilin. Key regulator of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus.<ref>PMID:11123801</ref> <ref>PMID:11506361</ref> | + | [https://www.uniprot.org/uniprot/FIMB1_ARATH FIMB1_ARATH] Cross-links actin filaments (F-actin) in a calcium independent manner. Stabilizes and prevents F-actin depolymerization mediated by profilin. Key regulator of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus.<ref>PMID:11123801</ref> <ref>PMID:11506361</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Almo, S C]] | + | [[Category: Almo SC]] |
| - | [[Category: Burley, S K]] | + | [[Category: Burley SK]] |
| - | [[Category: Klein, M G]] | + | [[Category: Klein MG]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Shi W]] |
| - | [[Category: Shi, W]] | + | [[Category: Tseng Y]] |
| - | [[Category: Tseng, Y]] | + | [[Category: Wirtz D]] |
| - | [[Category: Wirtz, D]] | + | |
| - | [[Category: Calponin homology]]
| + | |
| - | [[Category: F-actin-crosslinking]]
| + | |
| - | [[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
FIMB1_ARATH Cross-links actin filaments (F-actin) in a calcium independent manner. Stabilizes and prevents F-actin depolymerization mediated by profilin. Key regulator of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus.[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 PubMed
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.
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
- ↑ Kovar DR, Staiger CJ, Weaver EA, McCurdy DW. AtFim1 is an actin filament crosslinking protein from Arabidopsis thaliana. Plant J. 2000 Dec;24(5):625-36. PMID:11123801
- ↑ Kovar DR, Gibbon BC, McCurdy DW, Staiger CJ. Fluorescently-labeled fimbrin decorates a dynamic actin filament network in live plant cells. Planta. 2001 Jul;213(3):390-5. PMID:11506361
- ↑ Klein MG, Shi W, Ramagopal U, Tseng Y, Wirtz D, Kovar DR, Staiger CJ, Almo SC. Structure of the actin crosslinking core of fimbrin. Structure. 2004 Jun;12(6):999-1013. PMID:15274920 doi:10.1016/j.str.2004.04.010
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