View source for 5bvr


==Actin binding domain of alpha-actinin from Schizosaccharomyces pombe==
<StructureSection load='5bvr' size='340' side='right'caption='[[5bvr]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5BVR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.46&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5bvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bvr OCA], [https://pdbe.org/5bvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bvr RCSB], [https://www.ebi.ac.uk/pdbsum/5bvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bvr ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5bvr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Addario B]]
[[Category: Backman L]]
[[Category: Persson K]]