6WG6

Crystal structure of human SMC1-SMC3 hinge domain heterodimer in north-open conformation

Summary for 6WG6

• Entry DOI: 10.2210/pdb6wg6/pdb
• Related: 6WG3 6WG4
• Descriptor: Structural maintenance of chromosomes protein, Structural maintenance of chromosomes protein 3, poly(dT) (3 entities in total)
• Functional Keywords: protein-dna complex, atpase, dna-binding protein, genome organization, sister chromatid cohesion, transcription regulation, cell cycle, cell cycle-dna complex, cell cycle/dna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 14
• Total formula weight: 342792.81

Authors

Shi, Z.B.,Yu, H. (deposition date: 2020-04-04, release date: 2020-05-20, Last modification date: 2023-10-18)

Primary citation

Shi, Z.,Gao, H.,Bai, X.C.,Yu, H.
Cryo-EM structure of the human cohesin-NIPBL-DNA complex.
Science, 368:1454-1459, 2020

PubMed Abstract: 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.

PubMed: 32409525
DOI: 10.1126/science.abb0981

Experimental method

X-RAY DIFFRACTION (3.54 Å)