6QPW
Structural basis of cohesin ring opening
Summary for 6QPW
| Entry DOI | 10.2210/pdb6qpw/pdb |
| EMDB information | 4616 |
| Descriptor | Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein, Sister chromatid cohesion protein 1, Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3, ... (6 entities in total) |
| Functional Keywords | chromatin, genome segregation, cohesin, cell cycle |
| Biological source | Chaetomium thermophilum var. thermophilum DSM 1495 More |
| Total number of polymer chains | 4 |
| Total formula weight | 141499.43 |
| Authors | Panne, D.,Muir, K.W.,Li, Y.,Weis, F. (deposition date: 2019-02-15, release date: 2020-02-05, Last modification date: 2020-03-18) |
| Primary citation | Muir, K.W.,Li, Y.,Weis, F.,Panne, D. The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening. Nat.Struct.Mol.Biol., 27:233-239, 2020 Cited by PubMed Abstract: 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-Å resolution cryo-electron microscopy structure of the ATPγS-bound, heterotrimeric cohesin ATPase head module and the 2.1-Å 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. PubMed: 32066964DOI: 10.1038/s41594-020-0379-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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