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Open data
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Basic information
| Entry | Database: PDB / ID: 7yqh | |||||||||||||||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of 8-subunit Smc5/6 | |||||||||||||||||||||||||||||||||||||||||||||
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Keywords | CELL CYCLE | |||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationSmc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / SUMO ligase activity / chromosome separation / Platelet degranulation / SUMOylation of DNA damage response and repair proteins / ATPase inhibitor activity / chromatin looping / Transferases; Acyltransferases; Aminoacyltransferases ...Smc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / SUMO ligase activity / chromosome separation / Platelet degranulation / SUMOylation of DNA damage response and repair proteins / ATPase inhibitor activity / chromatin looping / Transferases; Acyltransferases; Aminoacyltransferases / SUMO transferase activity / DNA damage tolerance / recombinational repair / regulation of telomere maintenance / protein sumoylation / protein serine/threonine kinase inhibitor activity / double-strand break repair via homologous recombination / RING-type E3 ubiquitin transferase / ubiquitin-protein transferase activity / nuclear envelope / single-stranded DNA binding / site of double-strand break / DNA recombination / damaged DNA binding / chromosome, telomeric region / DNA repair / ATP hydrolysis activity / mitochondrion / zinc ion binding / ATP binding / nucleus / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.6 Å | |||||||||||||||||||||||||||||||||||||||||||||
Authors | Qian, L. / Jun, Z. / Xiang, Z. / Tong, C. / Zhaoning, W. / Duo, J. / Zhenguo, C. / Lanfeng, W. | |||||||||||||||||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024Title: Cryo-EM structures of Smc5/6 in multiple states reveal its assembly and functional mechanisms. Authors: Qian Li / Jun Zhang / Cory Haluska / Xiang Zhang / Lei Wang / Guangfeng Liu / Zhaoning Wang / Duo Jin / Tong Cheng / Hongxia Wang / Yuan Tian / Xiangxi Wang / Lei Sun / Xiaolan Zhao / ...Authors: Qian Li / Jun Zhang / Cory Haluska / Xiang Zhang / Lei Wang / Guangfeng Liu / Zhaoning Wang / Duo Jin / Tong Cheng / Hongxia Wang / Yuan Tian / Xiangxi Wang / Lei Sun / Xiaolan Zhao / Zhenguo Chen / Lanfeng Wang / ![]() 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 ...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. | |||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7yqh.cif.gz | 756.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7yqh.ent.gz | 609.9 KB | Display | PDB format |
| PDBx/mmJSON format | 7yqh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7yqh_validation.pdf.gz | 842.1 KB | Display | wwPDB validaton report |
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| Full document | 7yqh_full_validation.pdf.gz | 915.1 KB | Display | |
| Data in XML | 7yqh_validation.xml.gz | 114.3 KB | Display | |
| Data in CIF | 7yqh_validation.cif.gz | 177.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yq/7yqh ftp://data.pdbj.org/pub/pdb/validation_reports/yq/7yqh | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 34025MC ![]() 7ylmC ![]() 7ymdC ![]() 8hqsC ![]() 8i13C ![]() 8i21C ![]() 8i4uC ![]() 8i4vC ![]() 8i4wC ![]() 8i4xC ![]() 8wjlC ![]() 8wjnC ![]() 8wjoC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Structural maintenance of chromosomes protein ... , 2 types, 2 molecules AB
| #1: Protein | Mass: 126237.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Protein | Mass: 128199.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 2 types, 2 molecules CD
| #3: Protein | Mass: 30388.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P38632, Transferases; Acyltransferases; Aminoacyltransferases |
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| #4: Protein | Mass: 53836.758 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Non-structural maintenance of chromosome element ... , 2 types, 2 molecules EG
| #5: Protein | Mass: 64079.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #7: Protein | Mass: 34005.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Non-structural maintenance of chromosomes element ... , 2 types, 2 molecules FH
| #6: Protein | Mass: 38373.387 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q07913, RING-type E3 ubiquitin transferase |
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| #8: Protein | Mass: 46195.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Details
| Has protein modification | N |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Cryo-EM structure of 8-subunit Smc5/6 / Type: COMPLEX / Entity ID: #1-#5, #8, #6-#7 / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: DARK FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 5.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1056147 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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