5mg8 | pdb_00005mg8

Crystal structure of the S.pombe Smc5/6 hinge domain

spinqualitylabelsall models 5mg8, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mg8 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SMC5_SCHPO] Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis. [SMC6_SCHPO] Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis. Publication Abstract from PubMed The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both 'latch' and 'hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex. Specialized interfaces of Smc5/6 control hinge stability and DNA association.,Alt A, Dang HQ, Wells OS, Polo LM, Smith MA, McGregor GA, Welte T, Lehmann AR, Pearl LH, Murray JM, Oliver AW Nat Commun. 2017 Jan 30;8:14011. doi: 10.1038/ncomms14011. PMID:28134253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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