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7YLM

Cryo-EM structure of 8-subunit Smc5/6 hinge region

Summary for 7YLM
Entry DOI10.2210/pdb7ylm/pdb
EMDB information33914
DescriptorStructural maintenance of chromosomes protein 5, SMC6 isoform 1, MMS21 isoform 1 (3 entities in total)
Functional Keywordscell cycle
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains3
Total formula weight284825.23
Authors
Qian, L.,Jun, Z.,Xiang, Z.,Wang, Z.,Tong, C.,Duo, J.,Zhenguo, C.,Wang, L. (deposition date: 2022-07-26, release date: 2024-01-31, Last modification date: 2024-07-03)
Primary citationLi, Q.,Zhang, J.,Haluska, C.,Zhang, X.,Wang, L.,Liu, G.,Wang, Z.,Jin, D.,Cheng, T.,Wang, H.,Tian, Y.,Wang, X.,Sun, L.,Zhao, X.,Chen, Z.,Wang, L.
Cryo-EM structures of Smc5/6 in multiple states reveal its assembly and functional mechanisms.
Nat.Struct.Mol.Biol., 2024
Cited by
PubMed Abstract: Smc5/6 is a member of the eukaryotic structural maintenance of chromosomes (SMC) family of complexes with important roles in genome maintenance and viral restriction. However, limited structural understanding of Smc5/6 hinders the elucidation of its diverse functions. Here, we report cryo-EM structures of the budding yeast Smc5/6 complex in eight-subunit, six-subunit and five-subunit states. Structural maps throughout the entire length of these complexes reveal modularity and key elements in complex assembly. We show that the non-SMC element (Nse)2 subunit supports the overall shape of the complex and uses a wedge motif to aid the stability and function of the complex. The Nse6 subunit features a flexible hook region for attachment to the Smc5 and Smc6 arm regions, contributing to the DNA repair roles of the complex. Our results also suggest a structural basis for the opposite effects of the Nse1-3-4 and Nse5-6 subcomplexes in regulating Smc5/6 ATPase activity. Collectively, our integrated structural and functional data provide a framework for understanding Smc5/6 assembly and function.
PubMed: 38890552
DOI: 10.1038/s41594-024-01319-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.17 Å)
Structure validation

226707

數據於2024-10-30公開中

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