4MLK

3.05A resolution structure of CT584 from Chlamydia trachomatis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.227 

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This is version 1.3 of the entry. See complete history


Literature

Structure of CT584 from Chlamydia trachomatis refined to 3.05 angstrom resolution.

Barta, M.L.Hickey, J.Kemege, K.E.Lovell, S.Battaile, K.P.Hefty, P.S.

(2013) Acta Crystallogr Sect F Struct Biol Cryst Commun 69: 1196-1201

  • DOI: https://doi.org/10.1107/S1744309113027371
  • Primary Citation of Related Structures:  
    4MLK

  • PubMed Abstract: 

    Chlamydia trachomatis is a major cause of various diseases, including blinding trachoma and pelvic inflammatory disease, and is the leading reported sexually transmitted bacterial infection worldwide. All pathogenic Chlamydiae spp. utilize a supramolecular syringe, or type III secretion system (T3SS), to inject proteins into their obligate host in order to propagate infection. Here, the structure of CT584, a T3SS-associated protein, that has been refined to a resolution of 3.05 Å is reported. The CT584 structure is a hexamer comprised of a trimer of dimers. The structure shares a high degree of similarity to the recently reported structure of an orthologous protein, Cpn0803, from Chlamydia pneumoniae, which highlights the highly conserved nature of this protein across these chlamydial species, despite different tissue tropism and disease pathology.


  • Organizational Affiliation

    Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CT584 protein194Chlamydia trachomatis L2/434/BuMutation(s): 0 
Gene Names: CTL0847
UniProt
Find proteins for A0A0H3MCR9 (Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B))
Explore A0A0H3MCR9 
Go to UniProtKB:  A0A0H3MCR9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H3MCR9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.227 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.236α = 90
b = 112.236β = 90
c = 82.072γ = 120
Software Package:
Software NamePurpose
SCALAdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
JDirectordata collection
XDSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-11-13
    Type: Initial release
  • Version 1.1: 2013-12-18
    Changes: Database references
  • Version 1.2: 2017-11-15
    Changes: Refinement description
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references