3DIN

Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.50 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.279 
  • R-Value Observed: 0.279 

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Literature

Structure of a complex of the ATPase SecA and the protein-translocation channel.

Zimmer, J.Nam, Y.Rapoport, T.A.

(2008) Nature 455: 936-943

  • DOI: https://doi.org/10.1038/nature07335
  • Primary Citation of Related Structures:  
    3DIN, 3DL8

  • PubMed Abstract: 

    Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement through the SecY channel could be achieved by the motion of a 'two-helix finger' of SecA inside the cytoplasmic funnel of SecY, and by the coordinated tightening and widening of SecA's clamp above the SecY pore. SecA binding generates a 'window' at the lateral gate of the SecY channel and it displaces the plug domain, preparing the channel for signal sequence binding and channel opening.


  • Organizational Affiliation

    Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein translocase subunit secAA,
E [auth B]
871Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: secATM_1578
Membrane Entity: Yes 
UniProt
Find proteins for Q9X1R4 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X1R4 
Go to UniProtKB:  Q9X1R4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X1R4
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Preprotein translocase subunit SecYB [auth C],
F
431Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: secYTM_1480
Membrane Entity: Yes 
UniProt
Find proteins for Q9X1I9 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X1I9 
Go to UniProtKB:  Q9X1I9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X1I9
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Preprotein translocase subunit secEC [auth D],
G
65Thermotoga maritima MSB8Mutation(s): 0 
Gene Names: secETM_0452
Membrane Entity: Yes 
UniProt
Find proteins for P35874 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore P35874 
Go to UniProtKB:  P35874
Entity Groups  
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UniProt GroupP35874
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Preprotein translocase subunit SecGD [auth E],
H
76Thermotoga sp. RQ2Mutation(s): 0 
Gene Names: secGTRQ2_0456
Membrane Entity: Yes 
UniProt
Find proteins for A0A0F6AK20 (Thermotoga sp. (strain RQ2))
Explore A0A0F6AK20 
Go to UniProtKB:  A0A0F6AK20
Entity Groups  
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UniProt GroupA0A0F6AK20
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 4.50 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.279 
  • R-Value Observed: 0.279 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.616α = 90
b = 156.003β = 90
c = 358.155γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
SOLVEphasing
DMphasing
CNSrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-10-07
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description