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3l51

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{{STRUCTURE_3l51| PDB=3l51 | SCENE= }}
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==Crystal Structure of the Mouse Condensin Hinge Domain==
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===Crystal Structure of the Mouse Condensin Hinge Domain===
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<StructureSection load='3l51' size='340' side='right' caption='[[3l51]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
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{{ABSTRACT_PUBMED_20139420}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3l51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L51 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=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMC2 (amino acids 506-666) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), SMC4 (amino acids 595-752) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3l51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l51 RCSB], [http://www.ebi.ac.uk/pdbsum/3l51 PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l5/3l51_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Structural Maintenance of Chromosomes (SMC) proteins are vital for a wide range of processes including chromosome structure and dynamics, gene regulation and DNA repair. Eukaryotes have three SMC complexes, consisting of heterodimeric pairs of six different SMC proteins along with several specific regulatory subunits. In addition to their other functions, all three SMC complexes play distinct roles in DNA repair. Cohesin (SMC1-SMC3) is involved in DNA double-strand break repair, condensin (SMC2-SMC4) participates in single-strand break (SSB) repair, and the SMC5-SMC6 complex functions in various DNA repair pathways. SMC proteins consist of N- and C-terminal domains that fold back onto each other to create an ATPase 'head' domain, connected to a central 'hinge' domain via long coiled-coils. The hinge domain mediates dimerization of SMC proteins and binds DNA, but it is not clear to what purpose this activity serves. We studied the structure and function of the condensin hinge domain from mouse. While the SMC hinge domain structure is largely conserved from prokaryotes to eukaryotes, its function seems to have diversified throughout the course of evolution. The condensin hinge domain preferentially binds single-stranded DNA. We propose that this activity plays a role in the SSB repair function of the condensin complex.
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==Function==
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Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins.,Griese JJ, Witte G, Hopfner KP Nucleic Acids Res. 2010 Jun;38(10):3454-65. Epub 2010 Feb 5. PMID:20139420<ref>PMID:20139420</ref>
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[[http://www.uniprot.org/uniprot/SMC2_MOUSE SMC2_MOUSE]] 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 (By similarity). [[http://www.uniprot.org/uniprot/SMC4_MOUSE SMC4_MOUSE]] 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 (By similarity).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3l51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L51 OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:020139420</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Griese, J J.]]
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[[Category: Griese, J J]]
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[[Category: Hopfner, K P.]]
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[[Category: Hopfner, K P]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Cell division]]

Revision as of 17:54, 18 December 2014

Crystal Structure of the Mouse Condensin Hinge Domain

3l51, resolution 1.51Å

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