6QJ0
Crystal structure of the C. thermophilum condensin Smc2 ATPase head (crystal form II)
Summary for 6QJ0
| Entry DOI | 10.2210/pdb6qj0/pdb |
| Descriptor | Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein (2 entities in total) |
| Functional Keywords | condensin smc complex atpase chromosome condensation loop extrusion, cell cycle |
| Biological source | Chaetomium thermophilum More |
| Total number of polymer chains | 1 |
| Total formula weight | 46311.61 |
| Authors | Hassler, M.,Haering, C.H. (deposition date: 2019-01-22, release date: 2019-07-03, Last modification date: 2024-05-15) |
| Primary citation | Hassler, M.,Shaltiel, I.A.,Kschonsak, M.,Simon, B.,Merkel, F.,Tharichen, L.,Bailey, H.J.,Macosek, J.,Bravo, S.,Metz, J.,Hennig, J.,Haering, C.H. Structural Basis of an Asymmetric Condensin ATPase Cycle. Mol.Cell, 74:1175-1188.e9, 2019 Cited by PubMed Abstract: The condensin protein complex plays a key role in the structural organization of genomes. How the ATPase activity of its SMC subunits drives large-scale changes in chromosome topology has remained unknown. Here we reconstruct, at near-atomic resolution, the sequence of events that take place during the condensin ATPase cycle. We show that ATP binding induces a conformational switch in the Smc4 head domain that releases its hitherto undescribed interaction with the Ycs4 HEAT-repeat subunit and promotes its engagement with the Smc2 head into an asymmetric heterodimer. SMC head dimerization subsequently enables nucleotide binding at the second active site and disengages the Brn1 kleisin subunit from the Smc2 coiled coil to open the condensin ring. These large-scale transitions in the condensin architecture lay out a mechanistic path for its ability to extrude DNA helices into large loop structures. PubMed: 31226277DOI: 10.1016/j.molcel.2019.03.037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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