1gxj

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<StructureSection load='1gxj' size='340' side='right'caption='[[1gxj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1gxj' size='340' side='right'caption='[[1gxj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1gxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1gxj]] is a 2 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=1GXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXJ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e69|1e69]], [[1gxk|1gxk]], [[1gxl|1gxl]]</div></td></tr>
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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]] 2&#8491;</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=1gxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxj OCA], [https://pdbe.org/1gxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxj RCSB], [https://www.ebi.ac.uk/pdbsum/1gxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxj ProSAT]</span></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=1gxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxj OCA], [https://pdbe.org/1gxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxj RCSB], [https://www.ebi.ac.uk/pdbsum/1gxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[https://www.uniprot.org/uniprot/Q9X0R4_THEMA Q9X0R4_THEMA] Required for chromosome condensation and partitioning.[HAMAP-Rule:MF_01894]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1gxj ConSurf].
</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=1gxj ConSurf].
<div style="clear:both"></div>
<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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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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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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<div class="pdbe-citations 1gxj" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Haering, C]]
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[[Category: Thermotoga maritima]]
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[[Category: Lowe, J]]
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[[Category: Haering C]]
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[[Category: Nasmyth, K]]
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[[Category: Lowe J]]
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[[Category: Anti parallel coiled coil]]
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[[Category: Nasmyth K]]
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[[Category: Chromosome segregation]]
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[[Category: Smc dimerisation domain]]
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[[Category: Smc protein]]
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Revision as of 11:25, 27 March 2024

SMC hinge domain from T. maritima w/o coiled coil

PDB ID 1gxj

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