3AQP

Crystal structure of SecDF, a translocon-associated membrane protein, from Thermus thrmophilus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.319 
  • R-Value Work: 0.298 
  • R-Value Observed: 0.299 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure and function of a membrane component SecDF that enhances protein export

Tsukazaki, T.Mori, H.Echizen, Y.Ishitani, R.Fukai, S.Tanaka, T.Perederina, A.Vassylyev, D.G.Kohno, T.Maturana, A.D.Ito, K.Nureki, O.

(2011) Nature 474: 235-238

  • DOI: https://doi.org/10.1038/nature09980
  • Primary Citation of Related Structures:  
    2RRN, 3AQO, 3AQP

  • PubMed Abstract: 

    Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by proton motive force and membrane-integrated SecDF, which associates with SecYEG. The role of SecDF has remained unclear, although it is proposed to function in later stages of translocation as well as in membrane protein biogenesis. Here, we determined the crystal structure of Thermus thermophilus SecDF at 3.3 Å resolution, revealing a pseudo-symmetrical, 12-helix transmembrane domain belonging to the RND superfamily and two major periplasmic domains, P1 and P4. Higher-resolution analysis of the periplasmic domains suggested that P1, which binds an unfolded protein, undergoes functionally important conformational changes. In vitro analyses identified an ATP-independent step of protein translocation that requires both SecDF and proton motive force. Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins. Therefore, we propose that SecDF functions as a membrane-integrated chaperone, powered by proton motive force, to achieve ATP-independent protein translocation.


  • Organizational Affiliation

    Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable SecDF protein-export membrane protein
A, B
741Thermus thermophilus HB8Mutation(s): 1 
Gene Names: SECDFTTHA0697
Membrane Entity: Yes 
UniProt
Find proteins for Q5SKE6 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SKE6 
Go to UniProtKB:  Q5SKE6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SKE6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.319 
  • R-Value Work: 0.298 
  • R-Value Observed: 0.299 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 140.636α = 90
b = 140.636β = 90
c = 160.563γ = 90
Software Package:
Software NamePurpose
MLPHAREphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2014-01-22
    Changes: Database references
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Refinement description