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5bvr

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'''Unreleased structure'''
 
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The entry 5bvr is ON HOLD
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==Actin binding domain of alpha-actinin from Schizosaccharomyces pombe==
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<StructureSection load='5bvr' size='340' side='right' caption='[[5bvr]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bvr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BVR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=5bvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bvr OCA], [http://pdbe.org/5bvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bvr RCSB], [http://www.ebi.ac.uk/pdbsum/5bvr PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/AIN1_SCHPO AIN1_SCHPO]] Binds to actin and is involved in actin-ring formation and organization. Plays a role in cytokinesis and is involved in septation.<ref>PMID:11294907</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The actin cytoskeleton plays a fundamental role in eukaryotic cells. Its reorganization is regulated by a plethora of actin-modulating proteins, such as a-actinin. In higher organisms, alpha-actinin is characterized by the presence of three distinct structural domains: an N-terminal actin-binding domain and a C-terminal region with EF-hand motif separated by a central rod domain with four spectrin repeats. Sequence analysis has revealed that the central rod domain of alpha-actinin from the fission yeast Schizosaccharomyces pombe consists of only two spectrin repeats. To obtain a firmer understanding of the structure and function of this unconventional alpha-actinin, we have cloned and characterized each structural domain. Our results show that this a-actinin isoform is capable of forming dimers and that the rod domain is required for this. However, its actin-binding and cross-linking activity appears less efficient compared to conventional alpha-actinins. The solved crystal structure of the actin-binding domain indicates that the closed state is stabilised by hydrogen bonds and a salt bridge not present in other alpha-actinins, which may reduce the affinity for actin.
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Authors: Persson, K., Backman, L., Addario, B.
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Characterisation of Schizosaccharomyces pombe alpha-actinin.,Addario B, Sandblad L, Persson K, Backman L PeerJ. 2016 Mar 28;4:e1858. doi: 10.7717/peerj.1858. eCollection 2016. PMID:27069798<ref>PMID:27069798</ref>
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Description: Actin binding domain of alpha-actinin from Schizosaccharomyces pombe
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Backman, L]]
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<div class="pdbe-citations 5bvr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Addario, B]]
[[Category: Addario, B]]
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[[Category: Backman, L]]
[[Category: Persson, K]]
[[Category: Persson, K]]
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[[Category: Alpha-actinin actin binding schizosaccharomyces pombe]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]

Revision as of 17:02, 10 May 2016

Actin binding domain of alpha-actinin from Schizosaccharomyces pombe

5bvr, resolution 1.46Å

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