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| | <StructureSection load='5bvr' size='340' side='right'caption='[[5bvr]], [[Resolution|resolution]] 1.46Å' scene=''> | | <StructureSection load='5bvr' size='340' side='right'caption='[[5bvr]], [[Resolution|resolution]] 1.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bvr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ain1, SPAC15A10.08 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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> |
| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bvr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Addario, B]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Backman, L]] | + | [[Category: Addario B]] |
| - | [[Category: Persson, K]] | + | [[Category: Backman L]] |
| - | [[Category: Alpha-actinin actin binding schizosaccharomyces pombe]] | + | [[Category: Persson K]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| Structural highlights
Function
AIN1_SCHPO Binds to actin and is involved in actin-ring formation and organization. Plays a role in cytokinesis and is involved in septation.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu JQ, Bahler J, Pringle JR. Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis. Mol Biol Cell. 2001 Apr;12(4):1061-77. PMID:11294907
- ↑ Addario B, Sandblad L, Persson K, Backman L. Characterisation of Schizosaccharomyces pombe alpha-actinin. PeerJ. 2016 Mar 28;4:e1858. doi: 10.7717/peerj.1858. eCollection 2016. PMID:27069798 doi:http://dx.doi.org/10.7717/peerj.1858
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