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3l51

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{{Seed}}
 
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[[Image:3l51.png|left|200px]]
 
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==Crystal Structure of the Mouse Condensin Hinge Domain==
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The line below this paragraph, containing "STRUCTURE_3l51", creates the "Structure Box" on the page.
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<StructureSection load='3l51' size='340' side='right' caption='[[3l51]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3l51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_3l51| PDB=3l51 | SCENE= }}
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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 LK3 transgenic mice]), SMC4 (amino acids 595-752) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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://pdbe.org/3l51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l51 RCSB], [http://www.ebi.ac.uk/pdbsum/3l51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l51 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== 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/main_output.php?pdb_ID=3l51 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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===Crystal Structure of the Mouse Condensin Hinge Domain===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20139420}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3l51" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20139420 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20139420}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Lk3 transgenic mice]]
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3L51 is a 2 chains structure with sequences 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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[[Category: Griese, J J]]
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[[Category: Hopfner, K P]]
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==Reference==
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<ref group="xtra">PMID:20139420</ref><references group="xtra"/>
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[[Category: Mus musculus]]
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[[Category: Griese, J J.]]
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[[Category: Hopfner, K P.]]
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[[Category: Cell cycle]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Cell division]]
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[[Category: Mitosis]]
[[Category: Mitosis]]
[[Category: Nucleus]]
[[Category: Nucleus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 09:41:16 2010''
 

Current revision

Crystal Structure of the Mouse Condensin Hinge Domain

3l51, resolution 1.51Å

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