Structural highlights
6wg4 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 6wg3 |
| Gene: | SMC1A (HUMAN), SMC3, BAM, BMH, CSPG6, SMC3L1 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
[SMC3_HUMAN] Cornelia de Lange syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Function
[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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sumara I, Vorlaufer E, Gieffers C, Peters BH, Peters JM. Characterization of vertebrate cohesin complexes and their regulation in prophase. J Cell Biol. 2000 Nov 13;151(4):749-62. PMID:11076961
- ↑ Terret ME, Sherwood R, Rahman S, Qin J, Jallepalli PV. Cohesin acetylation speeds the replication fork. Nature. 2009 Nov 12;462(7270):231-4. PMID:19907496 doi:nature08550
- ↑ Shi Z, Gao H, Bai XC, Yu H. Cryo-EM structure of the human cohesin-NIPBL-DNA complex. Science. 2020 May 14. pii: science.abb0981. doi: 10.1126/science.abb0981. PMID:32409525 doi:http://dx.doi.org/10.1126/science.abb0981
