1NL3

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal Structure of M. tuberculosis SecA, A Preprotein Translocating ATPase

Sharma, V.Arockiasamy, A.Ronning, D.R.Savva, C.G.Holzenburg, A.Braunstein, M.Jacobs Jr., W.R.Sacchettini, J.C.

(2003) Proc Natl Acad Sci U S A 100: 2243-2248

  • DOI: https://doi.org/10.1073/pnas.0538077100
  • Primary Citation of Related Structures:  
    1NKT, 1NL3

  • PubMed Abstract: 

    In bacteria, the majority of exported proteins are translocated by the Sec system, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to mediate protein translocation across the cytoplasmic membrane. SecA is an essential protein component of this system, containing the molecular motor that facilitates translocation. Here we report the three-dimensional structure of the SecA protein of Mycobacterium tuberculosis. Each subunit of the homodimer contains a "motor" domain and a translocation domain. The structure predicts that SecA can interact with the SecYEG pore and function as a molecular ratchet that uses ATP hydrolysis for physical movement of the preprotein. Knowledge of this structure provides a framework for further elucidation of the translocation process.


  • Organizational Affiliation

    Center for Structural Biology, Institute of Biosciences and Technology, Houston, TX 77030, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PREPROTEIN TRANSLOCASE SECA 1 SUBUNIT
A, B
922Mycobacterium tuberculosisMutation(s): 0 
Gene Names: SECA1 OR SECA OR RV3240C
UniProt
Find proteins for P9WGP5 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WGP5 
Go to UniProtKB:  P9WGP5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WGP5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 
  • Space Group: P 62 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 206.196α = 90
b = 206.196β = 90
c = 295.412γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SHARPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2003-03-04
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references