7C98

Human DMC1 post-synaptic complexes


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.47 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Identification of fidelity-governing factors in human recombinases DMC1 and RAD51 from cryo-EM structures.

Luo, S.C.Yeh, H.Y.Lan, W.H.Wu, Y.M.Yang, C.H.Chang, H.Y.Su, G.C.Lee, C.Y.Wu, W.J.Li, H.W.Ho, M.C.Chi, P.Tsai, M.D.

(2021) Nat Commun 12: 115-115

  • DOI: https://doi.org/10.1038/s41467-020-20258-1
  • Primary Citation of Related Structures:  
    7C98, 7C99, 7C9A, 7C9C, 7CGY

  • PubMed Abstract: 

    Both high-fidelity and mismatch-tolerant recombination, catalyzed by RAD51 and DMC1 recombinases, respectively, are indispensable for genomic integrity. Here, we use cryo-EM, MD simulation and functional analysis to elucidate the structural basis for the mismatch tolerance of DMC1. Structural analysis of DMC1 presynaptic and postsynaptic complexes suggested that the lineage-specific Loop 1 Gln244 (Met243 in RAD51) may help stabilize DNA backbone, whereas Loop 2 Pro274 and Gly275 (Val273/Asp274 in RAD51) may provide an open "triplet gate" for mismatch tolerance. In support, DMC1-Q244M displayed marked increase in DNA dynamics, leading to unobservable DNA map. MD simulation showed highly dispersive mismatched DNA ensemble in RAD51 but well-converged DNA in DMC1 and RAD51-V273P/D274G. Replacing Loop 1 or Loop 2 residues in DMC1 with RAD51 counterparts enhanced DMC1 fidelity, while reciprocal mutations in RAD51 attenuated its fidelity. Our results show that three Loop 1/Loop 2 residues jointly enact contrasting fidelities of DNA recombinases.


  • Organizational Affiliation

    Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Meiotic recombination protein DMC1/LIM15 homolog
A, B, C
340Homo sapiensMutation(s): 0 
Gene Names: DMC1DMC1HLIM15
UniProt & NIH Common Fund Data Resources
Find proteins for Q14565 (Homo sapiens)
Explore Q14565 
Go to UniProtKB:  Q14565
PHAROS:  Q14565
GTEx:  ENSG00000100206 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ14565
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')9synthetic construct
Sequence Annotations
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  • Reference Sequence

Find similar nucleic acids by:  Sequence   |   3D Structure  

Entity ID: 3
MoleculeChains LengthOrganismImage
DNA (5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*A)-3')9synthetic construct
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.47 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTCoot0.8.9.2
MODEL REFINEMENTRosetta3.9
RECONSTRUCTIONRELION3.0

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Academia Sinica (Taiwan)TaiwanAS-KPQ-109-TPP2
Academia Sinica (Taiwan)TaiwanAS-CFII-108-110
Academia Sinica (Taiwan)TaiwanAS-KPQ-105-TPP

Revision History  (Full details and data files)

  • Version 1.0: 2020-11-18
    Type: Initial release
  • Version 1.1: 2020-11-25
    Changes: Structure summary
  • Version 1.2: 2021-01-27
    Changes: Database references
  • Version 1.3: 2024-03-27
    Changes: Data collection, Database references