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1gxk

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(New page: 200px<br /><applet load="1gxk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxk, resolution 3.0&Aring;" /> '''SMC HINGE DOMAIN FROM...)
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[[Image:1gxk.gif|left|200px]]<br /><applet load="1gxk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gxk, resolution 3.0&Aring;" />
 
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'''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM'''<br />
 
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==Overview==
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==SMC hinge domain from T. maritima w/o coiled coil, P212121 crystal form==
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Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3), proteins. The crystal structure of a bacterial SMC "hinge" region along, with EM studies and biochemical experiments on yeast Smc1 and Smc3, proteins show that SMC protamers fold up individually into rod-shaped, molecules. A 45 nm long intramolecular coiled coil separates the hinge, region from the ATPase-containing "head" domain. Smc1 and Smc3 bind to, each other via heterotypic interactions between their hinges to form a, V-shaped heterodimer. The two heads of the V-shaped dimer are connected by, different ends of the cleavable Scc1 subunit. Cohesin therefore forms a, large proteinaceous loop within which sister chromatids might be entrapped, after DNA replication.
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<StructureSection load='1gxk' size='340' side='right'caption='[[1gxk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gxk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxk OCA], [https://pdbe.org/1gxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxk RCSB], [https://www.ebi.ac.uk/pdbsum/1gxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9X0R4_THEMA Q9X0R4_THEMA] Required for chromosome condensation and partitioning.[HAMAP-Rule:MF_01894]
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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/gx/1gxk_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=1gxk 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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Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of a bacterial SMC "hinge" region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers fold up individually into rod-shaped molecules. A 45 nm long intramolecular coiled coil separates the hinge region from the ATPase-containing "head" domain. Smc1 and Smc3 bind to each other via heterotypic interactions between their hinges to form a V-shaped heterodimer. The two heads of the V-shaped dimer are connected by different ends of the cleavable Scc1 subunit. Cohesin therefore forms a large proteinaceous loop within which sister chromatids might be entrapped after DNA replication.
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==About this Structure==
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Molecular architecture of SMC proteins and the yeast cohesin complex.,Haering CH, Lowe J, Hochwagen A, Nasmyth K Mol Cell. 2002 Apr;9(4):773-88. PMID:11983169<ref>PMID:11983169</ref>
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1GXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GXK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Molecular architecture of SMC proteins and the yeast cohesin complex., Haering CH, Lowe J, Hochwagen A, Nasmyth K, Mol Cell. 2002 Apr;9(4):773-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11983169 11983169]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1gxk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Haering, C.]]
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[[Category: Haering C]]
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[[Category: Lowe, J.]]
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[[Category: Lowe J]]
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[[Category: Nasmyth, K.]]
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[[Category: Nasmyth K]]
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[[Category: anti parallel coiled coil]]
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[[Category: complete proteome.]]
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[[Category: smc dimerisation domain]]
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[[Category: smc proteins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:56:00 2007''
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Current revision

SMC hinge domain from T. maritima w/o coiled coil, P212121 crystal form

PDB ID 1gxk

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