5YZ0

Cryo-EM Structure of human ATR-ATRIP complex

  • Classification: CELL CYCLE
  • Organism(s): Homo sapiens
  • Expression System: Homo sapiens
  • Mutation(s): No 

  • Deposited: 2017-12-11 Released: 2018-01-31 
  • Deposition Author(s): Rao, Q., Liu, M., Tian, Y., Wu, Z., Wang, H., Wang, J., Xu, Y.
  • Funding Organization(s): Ministry of Science and Technology (China), Strategic Priority Research Program of Chinese Academy of Sciences(CAS)), National Natural Science Foundation of China, Beijing Municipal Science & Technology Commission

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.70 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Cryo-EM structure of human ATR-ATRIP complex.

Rao, Q.Liu, M.Tian, Y.Wu, Z.Hao, Y.Song, L.Qin, Z.Ding, C.Wang, H.W.Wang, J.Xu, Y.

(2018) Cell Res 28: 143-156

  • DOI: https://doi.org/10.1038/cr.2017.158
  • Primary Citation of Related Structures:  
    5YZ0

  • PubMed Abstract: 

    ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, we determined the cryo-electron microscopy (EM) structure of the human ATR-ATRIP complex at 4.7 Å resolution and built an atomic model of the C-terminal catalytic core of ATR (residues 1 521-2 644) at 3.9 Å resolution. The complex adopts a hollow "heart" shape, consisting of two ATR monomers in distinct conformations. The EM map for ATRIP reveals 14 HEAT repeats in an extended "S" shape. The conformational flexibility of ATR allows ATRIP to properly lock the N-termini of the two ATR monomers to favor ATR-ATRIP complex formation and functional diversity. The isolated "head-head" and "tail-tail" each adopts a pseudo 2-fold symmetry. The catalytic pockets face outward and substrate access is not restricted by inhibitory elements. Our studies provide a structural basis for understanding the assembly of the ATR-ATRIP complex and a framework for characterizing ATR-mediated DNA repair pathways.


  • Organizational Affiliation

    Fudan University Shanghai Cancer Center, Institute of Biomedical Sciences, Shanghai Medical College of Fudan University, Shanghai 200032, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase ATR
A, B
2,644Homo sapiensMutation(s): 0 
Gene Names: ATRFRP1
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q13535 (Homo sapiens)
Explore Q13535 
Go to UniProtKB:  Q13535
PHAROS:  Q13535
GTEx:  ENSG00000175054 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13535
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ATR-interacting protein
C, D
791Homo sapiensMutation(s): 0 
Gene Names: ATRIPAGS1
UniProt & NIH Common Fund Data Resources
Find proteins for Q8WXE1 (Homo sapiens)
Explore Q8WXE1 
Go to UniProtKB:  Q8WXE1
PHAROS:  Q8WXE1
GTEx:  ENSG00000164053 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8WXE1
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.70 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Ministry of Science and Technology (China)China2016YFA0500700
Ministry of Science and Technology (China)China2016YFA0501100
Strategic Priority Research Program of Chinese Academy of Sciences(CAS))ChinaXDB08000000
National Natural Science Foundation of ChinaChinaU1432242
National Natural Science Foundation of ChinaChina31425008
National Natural Science Foundation of ChinaChina91419301
Beijing Municipal Science & Technology CommissionChinaZ161100000116034

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-31
    Type: Initial release
  • Version 1.1: 2018-03-21
    Changes: Database references
  • Version 1.2: 2019-11-06
    Changes: Data collection, Other