Structural highlights
6qpw is a 4 chain structure with sequence from Baker's yeast and Chatd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Gene: | CTHT_0066330 (CHATD), MCD1, PDS3, RHC21, SCC1, YDL003W, YD8119.04 (Baker's yeast), SMC3, YJL074C, J1049 (Baker's yeast), CTHT_0066330 (Baker's yeast) |
| Experimental data: | Check |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SCC1_YEAST] Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.[1] [2] [3] [4] [SMC3_YEAST] Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms 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.
Publication Abstract from PubMed
Genome regulation requires control of chromosome organization by SMC-kleisin complexes. The cohesin complex contains the Smc1 and Smc3 subunits that associate with the kleisin Scc1 to form a ring-shaped complex that can topologically engage chromatin to regulate chromatin structure. Release from chromatin involves opening of the ring at the Smc3-Scc1 interface in a reaction that is controlled by acetylation and engagement of the Smc ATPase head domains. To understand the underlying molecular mechanisms, we have determined the 3.2-A resolution cryo-electron microscopy structure of the ATPgammaS-bound, heterotrimeric cohesin ATPase head module and the 2.1-A resolution crystal structure of a nucleotide-free Smc1-Scc1 subcomplex from Saccharomyces cerevisiae and Chaetomium thermophilium. We found that ATP-binding and Smc1-Smc3 heterodimerization promote conformational changes within the ATPase that are transmitted to the Smc coiled-coil domains. Remodeling of the coiled-coil domain of Smc3 abrogates the binding surface for Scc1, thus leading to ring opening at the Smc3-Scc1 interface.
The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening.,Muir KW, Li Y, Weis F, Panne D Nat Struct Mol Biol. 2020 Feb 17. pii: 10.1038/s41594-020-0379-7. doi:, 10.1038/s41594-020-0379-7. PMID:32066964[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Michaelis C, Ciosk R, Nasmyth K. Cohesins: chromosomal proteins that prevent premature separation of sister chromatids. Cell. 1997 Oct 3;91(1):35-45. PMID:9335333
- ↑ Guacci V, Koshland D, Strunnikov A. A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae. Cell. 1997 Oct 3;91(1):47-57. PMID:9335334
- ↑ Heo SJ, Tatebayashi K, Kato J, Ikeda H. The RHC21 gene of budding yeast, a homologue of the fission yeast rad21+ gene, is essential for chromosome segregation. Mol Gen Genet. 1998 Jan;257(2):149-56. PMID:9491073
- ↑ Uhlmann F, Lottspeich F, Nasmyth K. Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1. Nature. 1999 Jul 1;400(6739):37-42. PMID:10403247 doi:http://dx.doi.org/10.1038/21831
- ↑ Muir KW, Li Y, Weis F, Panne D. The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening. Nat Struct Mol Biol. 2020 Feb 17. pii: 10.1038/s41594-020-0379-7. doi:, 10.1038/s41594-020-0379-7. PMID:32066964 doi:http://dx.doi.org/10.1038/s41594-020-0379-7