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| | <StructureSection load='4rsi' size='340' side='right'caption='[[4rsi]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='4rsi' size='340' side='right'caption='[[4rsi]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rsi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RSI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RSI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RSI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rsj|4rsj]]</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=4rsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rsi OCA], [https://pdbe.org/4rsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rsi RCSB], [https://www.ebi.ac.uk/pdbsum/4rsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rsi ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Saccharomyces cerevisiae, SMC2, YFR031C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), L9449.5, Saccharomyces cerevisiae, SMC4, YLR086W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4rsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rsi OCA], [http://pdbe.org/4rsi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rsi RCSB], [http://www.ebi.ac.uk/pdbsum/4rsi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rsi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SMC2_YEAST SMC2_YEAST]] Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. [[http://www.uniprot.org/uniprot/SMC4_YEAST SMC4_YEAST]] Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. | + | [https://www.uniprot.org/uniprot/SMC2_YEAST SMC2_YEAST] Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. |
| | <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: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oh, B H]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Shin, H C]] | + | [[Category: Oh BH]] |
| - | [[Category: Soh, Y M]] | + | [[Category: Shin HC]] |
| - | [[Category: Cell cycle]] | + | [[Category: Soh YM]] |
| - | [[Category: Chromosomal condensation]]
| + | |
| - | [[Category: Smc hinge domain with coiled coil]]
| + | |
| Structural highlights
Function
SMC2_YEAST Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Publication Abstract from PubMed
SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge" dimerization domain with an ATP-regulated "head" dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome.
Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding.,Soh YM, Burmann F, Shin HC, Oda T, Jin KS, Toseland CP, Kim C, Lee H, Kim SJ, Kong MS, Durand-Diebold ML, Kim YG, Kim HM, Lee NK, Sato M, Oh BH, Gruber S Mol Cell. 2015 Jan 22;57(2):290-303. doi: 10.1016/j.molcel.2014.11.023. Epub 2014, Dec 31. PMID:25557547[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Soh YM, Burmann F, Shin HC, Oda T, Jin KS, Toseland CP, Kim C, Lee H, Kim SJ, Kong MS, Durand-Diebold ML, Kim YG, Kim HM, Lee NK, Sato M, Oh BH, Gruber S. Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding. Mol Cell. 2015 Jan 22;57(2):290-303. doi: 10.1016/j.molcel.2014.11.023. Epub 2014, Dec 31. PMID:25557547 doi:http://dx.doi.org/10.1016/j.molcel.2014.11.023
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