6wg4
From Proteopedia
(Difference between revisions)
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==Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation== | ==Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation== | ||
| - | <StructureSection load='6wg4' size='340' side='right'caption='[[6wg4]]' scene=''> | + | <StructureSection load='6wg4' size='340' side='right'caption='[[6wg4]], [[Resolution|resolution]] 2.31Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WG4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WG4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6wg4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WG4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WG4 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg4 OCA], [http://pdbe.org/6wg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wg4 RCSB], [http://www.ebi.ac.uk/pdbsum/6wg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg4 ProSAT]</span></td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6wg3|6wg3]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMC1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SMC3, BAM, BMH, CSPG6, SMC3L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg4 OCA], [http://pdbe.org/6wg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wg4 RCSB], [http://www.ebi.ac.uk/pdbsum/6wg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/SMC3_HUMAN SMC3_HUMAN]] Cornelia de Lange syndrome. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SMC3_HUMAN SMC3_HUMAN]] Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement.<ref>PMID:11076961</ref> <ref>PMID:19907496</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As a ring-shaped ATPase machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister-chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo-electron microscopy, we determine the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72-base pair DNA. NIPBL and DNA promote the engagement of cohesin's ATPase head domains and ATP binding. The hinge domains of cohesin adopt an "open washer" conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA, and provides insight into DNA entrapment by cohesin. | ||
| + | |||
| + | Cryo-EM structure of the human cohesin-NIPBL-DNA complex.,Shi Z, Gao H, Bai XC, Yu H Science. 2020 May 14. pii: science.abb0981. doi: 10.1126/science.abb0981. PMID:32409525<ref>PMID:32409525</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6wg4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Shi | + | [[Category: Shi, Z B]] |
| - | [[Category: Yu H]] | + | [[Category: Yu, H]] |
| + | [[Category: Atpase]] | ||
| + | [[Category: Cell cycle]] | ||
| + | [[Category: Dna-binding protein]] | ||
| + | [[Category: Genome organization]] | ||
| + | [[Category: Sister chromatid cohesion]] | ||
| + | [[Category: Transcription regulation]] | ||
Revision as of 07:41, 27 May 2020
Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation
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