5MG8

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

Summary for 5MG8

• Entry DOI: 10.2210/pdb5mg8/pdb
• Descriptor: Structural maintenance of chromosomes protein 5, Structural maintenance of chromosomes protein 6, SULFATE ION, ... (5 entities in total)
• Functional Keywords: smc, structural maintenance of chromosomes, hinge domain, smc5, smc6, smc5/6, recombination
• Biological source: Schizosaccharomyces pombe (Fission yeast); More
• Cellular location: Nucleus : O13710 P53692
• Total number of polymer chains: 4
• Total formula weight: 148924.83

Authors

Alt, A.,Pearl, L.H.,Oliver, A.W. (deposition date: 2016-11-21, release date: 2017-02-08, Last modification date: 2024-05-08)

Primary citation

Alt, A.,Dang, H.Q.,Wells, O.S.,Polo, L.M.,Smith, M.A.,McGregor, G.A.,Welte, T.,Lehmann, A.R.,Pearl, L.H.,Murray, J.M.,Oliver, A.W.
Specialized interfaces of Smc5/6 control hinge stability and DNA association.
Nat Commun, 8:14011-14011, 2017

PubMed Abstract: 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.

PubMed: 28134253
DOI: 10.1038/ncomms14011

Experimental method

X-RAY DIFFRACTION (2.75 Å)