6qj4

Crystal structure of the C. thermophilum condensin Ycs4-Brn1 subcomplex bound to the Smc4 ATPase head in complex with the C-terminal domain of Brn1

spinqualitylabelsall models 6qj4, resolution 5.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qj4 is a 5 chain structure with sequence from Chaetomium thermophilum and Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 5.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SB82_CHATD Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.[PIRNR:PIRNR017127] Publication Abstract from PubMed 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. Structural Basis of an Asymmetric Condensin ATPase Cycle.,Hassler M, Shaltiel IA, Kschonsak M, Simon B, Merkel F, Tharichen L, Bailey HJ, Macosek J, Bravo S, Metz J, Hennig J, Haering CH Mol Cell. 2019 Jun 20;74(6):1175-1188.e9. doi: 10.1016/j.molcel.2019.03.037. PMID:31226277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Condensin

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