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TitleThe structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 3, Page 233-239, Year 2020
Publish dateFeb 17, 2020
AuthorsKyle W Muir / Yan Li / Felix Weis / Daniel Panne /
PubMed AbstractGenome 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- ...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.
External linksNat Struct Mol Biol / PubMed:32066964 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 3.3 Å
Structure data

4616

6qpw

EMDB-4616, PDB-6qpw:
Structural basis of cohesin ring opening
Method: EM (single particle) / Resolution: 3.3 Å

PDB-6qpq:
The structure of the cohesin head module elucidates the mechanism of ring opening
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

Source
  • Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
  • Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
  • chaetomium thermophilum var. thermophilum dsm 1495 (fungus)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsCELL CYCLE / Cohesin / cell division / genome regulation / sister chromatid cohesion / SMC / kleisin / Chromatin / genome segregation

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