2VDA

Solution structure of the SecA-signal peptide complex


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Basis for Signal-Sequence Recognition by the Translocase Motor Seca as Determined by NMR

Gelis, I.Bonvin, A.M.J.J.Keramisanou, D.Koukaki, M.Gouridis, G.Karamanou, S.Economou, A.Kalodimos, C.G.

(2007) Cell 131: 756

  • DOI: https://doi.org/10.1016/j.cell.2007.09.039
  • Primary Citation of Related Structures:  
    2VDA

  • PubMed Abstract: 

    Recognition of signal sequences by cognate receptors controls the entry of virtually all proteins to export pathways. Despite its importance, this process remains poorly understood. Here, we present the solution structure of a signal peptide bound to SecA, the 204 kDa ATPase motor of the Sec translocase. Upon encounter, the signal peptide forms an alpha-helix that inserts into a flexible and elongated groove in SecA. The mode of binding is bimodal, with both hydrophobic and electrostatic interactions mediating recognition. The same groove is used by SecA to recognize a diverse set of signal sequences. Impairment of the signal-peptide binding to SecA results in significant translocation defects. The C-terminal tail of SecA occludes the groove and inhibits signal-peptide binding, but autoinhibition is relieved by the SecB chaperone. Finally, it is shown that SecA interconverts between two conformations in solution, suggesting a simple mechanism for polypeptide translocation.


  • Organizational Affiliation

    Department of Chemistry, Rutgers University, Newark, NJ 07102, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSLOCASE SUBUNIT SECA828Escherichia coliMutation(s): 0 
UniProt
Find proteins for P10408 (Escherichia coli (strain K12))
Explore P10408 
Go to UniProtKB:  P10408
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Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10408
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MALTOPORIN28Escherichia coliMutation(s): 0 
UniProt
Find proteins for Q8CVI4 (Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC))
Explore Q8CVI4 
Go to UniProtKB:  Q8CVI4
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UniProt GroupQ8CVI4
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-11-27
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Source and taxonomy