6WGE
Cryo-EM structure of human Cohesin-NIPBL-DNA complex without STAG1
Summary for 6WGE
| Entry DOI | 10.2210/pdb6wge/pdb |
| EMDB information | 21663 |
| Descriptor | Structural maintenance of chromosomes protein 1A, Structural maintenance of chromosomes protein 3, Double-strand-break repair protein rad21 homolog, ... (8 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 | 6 |
| Total formula weight | 571108.31 |
| Authors | |
| 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 Cited by 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: 32409525DOI: 10.1126/science.abb0981 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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