7QCD
CryoEM structure of the Smc5/6-holocomplex (composite structure)
Summary for 7QCD
| Entry DOI | 10.2210/pdb7qcd/pdb |
| EMDB information | 13893 13894 13895 |
| Descriptor | Structural maintenance of chromosomes protein 5, Structural maintenance of chromosomes protein 6, E3 SUMO-protein ligase MMS21, ... (7 entities in total) |
| Functional Keywords | structural maintenance of chromosomes, smc, holo-complex, recombination, stalled replication fork |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 6 |
| Total formula weight | 442838.70 |
| Authors | Hallett, S.T.,Oliver, A.W. (deposition date: 2021-11-23, release date: 2022-09-21, Last modification date: 2024-07-17) |
| Primary citation | Hallett, S.T.,Campbell Harry, I.,Schellenberger, P.,Zhou, L.,Cronin, N.B.,Baxter, J.,Etheridge, T.J.,Murray, J.M.,Oliver, A.W. Cryo-EM structure of the Smc5/6 holo-complex. Nucleic Acids Res., 50:9505-9520, 2022 Cited by PubMed Abstract: The Smc5/6 complex plays an essential role in the resolution of recombination intermediates formed during mitosis or meiosis, or as a result of the cellular response to replication stress. It also functions as a restriction factor preventing viral replication. Here, we report the cryogenic EM (cryo-EM) structure of the six-subunit budding yeast Smc5/6 holo-complex, reconstituted from recombinant proteins expressed in insect cells - providing both an architectural overview of the entire complex and an understanding of how the Nse1/3/4 subcomplex binds to the hetero-dimeric SMC protein core. In addition, we demonstrate that a region within the head domain of Smc5, equivalent to the 'W-loop' of Smc4 or 'F-loop' of Smc1, mediates an important interaction with Nse1. Notably, mutations that alter the surface-charge profile of the region of Nse1 which accepts the Smc5-loop, lead to a slow-growth phenotype and a global reduction in the chromatin-associated fraction of the Smc5/6 complex, as judged by single molecule localisation microscopy experiments in live yeast. Moreover, when taken together, our data indicates functional equivalence between the structurally unrelated KITE and HAWK accessory subunits associated with SMC complexes. PubMed: 35993814DOI: 10.1093/nar/gkac692 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8 Å) |
Structure validation
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