1HV8

CRYSTAL STRUCTURE OF A DEAD BOX PROTEIN FROM THE HYPERTHERMOPHILE METHANOCOCCUS JANNASCHII


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.316 
  • R-Value Work: 0.270 

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This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii.

Story, R.M.Li, H.Abelson, J.N.

(2001) Proc Natl Acad Sci U S A 98: 1465-1470

  • DOI: https://doi.org/10.1073/pnas.98.4.1465
  • Primary Citation of Related Structures:  
    1HV8

  • PubMed Abstract: 

    We have determined the structure of a DEAD box putative RNA helicase from the hyperthermophile Methanococcus jannaschii. Like other helicases, the protein contains two alpha/beta domains, each with a recA-like topology. Unlike other helicases, the protein exists as a dimer in the crystal. Through an interaction that resembles the dimer interface of insulin, the amino-terminal domain's 7-strand beta-sheet is extended to 14 strands across the two molecules. Motifs conserved in the DEAD box family cluster in the cleft between domains, and many of their functions can be deduced by mutational data and by comparison with other helicase structures. Several lines of evidence suggest that motif III Ser-Ala-Thr may be involved in binding RNA.


  • Organizational Affiliation

    California Institute of Technology, Division of Biology 147-75, Pasadena, CA 91125, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PUTATIVE ATP-DEPENDENT RNA HELICASE MJ0669
A, B
367Methanocaldococcus jannaschiiMutation(s): 11 
UniProt
Find proteins for Q58083 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440))
Explore Q58083 
Go to UniProtKB:  Q58083
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ58083
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.316 
  • R-Value Work: 0.270 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 109.132α = 90
b = 131.45β = 90
c = 131.829γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
CNSrefinement
DMphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-02-21
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance