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Structure paper

TitleCryo-EM structure of the human cohesin-NIPBL-DNA complex.
Journal, issue, pagesScience, Vol. 368, Issue 6498, Page 1454-1459, Year 2020
Publish dateJun 26, 2020
AuthorsZhubing Shi / Haishan Gao / Xiao-Chen Bai / Hongtao Yu /
PubMed AbstractAs a ring-shaped adenosine triphosphatase (ATPase) machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister chromatid cohesion by topologically entrapping DNA. How ...As a ring-shaped adenosine triphosphatase (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 (cryo-EM), we determined 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.
External linksScience / PubMed:32409525
MethodsEM (single particle) / X-ray diffraction
Resolution2.31 - 5.3 Å
Structure data

21658

6wg3

EMDB-21658, PDB-6wg3:
Cryo-EM structure of human Cohesin-NIPBL-DNA complex
Method: EM (single particle) / Resolution: 5.3 Å

21663

6wge

EMDB-21663, PDB-6wge:
Cryo-EM structure of human Cohesin-NIPBL-DNA complex without STAG1
Method: EM (single particle) / Resolution: 3.9 Å

PDB-6wg4:
Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-6wg6:
Crystal structure of human SMC1-SMC3 hinge domain heterodimer in north-open conformation
Method: X-RAY DIFFRACTION / Resolution: 3.54 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER / Water

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCELL CYCLE/DNA / Protein-DNA complex / ATPase / DNA-binding protein / Genome organization / Sister chromatid cohesion / Transcription regulation / CELL CYCLE / CELL CYCLE-DNA complex

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