3MCB

Crystal structure of NAC domains of human nascent polypeptide-associated complex (NAC)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.194 

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This is version 1.4 of the entry. See complete history


Literature

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit

Wang, L.F.Zhang, W.C.Wang, L.Zhang, X.J.C.Li, X.M.Rao, Z.

(2010) Protein Cell 1: 406-416

  • DOI: https://doi.org/10.1007/s13238-010-0049-3
  • Primary Citation of Related Structures:  
    3MCB, 3MCE

  • PubMed Abstract: 

    Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.


  • Organizational Affiliation

    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Nascent polypeptide-associated complex subunit alpha54Homo sapiensMutation(s): 0 
Gene Names: Alpha NACHSD48NACA
UniProt & NIH Common Fund Data Resources
Find proteins for Q13765 (Homo sapiens)
Explore Q13765 
Go to UniProtKB:  Q13765
PHAROS:  Q13765
GTEx:  ENSG00000196531 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13765
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription factor BTF358Homo sapiensMutation(s): 0 
Gene Names: Beta NAC (BTF3b)BTF3NACBOK/SW-cl.8
UniProt & NIH Common Fund Data Resources
Find proteins for P20290 (Homo sapiens)
Explore P20290 
Go to UniProtKB:  P20290
PHAROS:  P20290
GTEx:  ENSG00000145741 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP20290
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.194 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.794α = 90
b = 59.794β = 90
c = 156.763γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
ADSCdata collection
HKL-2000data reduction
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-07-14
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2012-04-11
    Changes: Database references
  • Version 1.3: 2017-11-08
    Changes: Refinement description
  • Version 1.4: 2024-03-20
    Changes: Data collection, Database references, Derived calculations