5Z8O

Structural of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.210 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis.

Zheng, S.Zhou, Y.Fleming, J.Zhou, Y.Zhang, M.Li, S.Li, H.Sun, B.Liu, W.Bi, L.

(2018) FEBS Lett 592: 1445-1457

  • DOI: https://doi.org/10.1002/1873-3468.13024
  • Primary Citation of Related Structures:  
    5Z8O

  • PubMed Abstract: 

    Mycobacterium tuberculosis is a notorious pathogen that continues to threaten human health. Rv0164, an antigen of both T- and B cells conserved across mycobacteria, and MSMEG_0129, its close homolog in Mycobacterium smegmatis, are predicted members of the START domain superfamily, but their molecular function is unknown. Here, gene knockout studies demonstrate MSMEG_0129 is essential for bacterial growth, suggesting Rv0164 may be a potential drug target. The MSMEG_0129 crystal structure determined at 1.95 Å reveals a fold similar to that in polyketide aromatase/cyclases ZhuI and TcmN from Streptomyces sp. Structural comparisons and docking simulations, however, infer that MSMEG_0129 and Rv0164 are unlikely to catalyze polyketide aromatization/cyclization, but probably play an irreplaceable role during mycobacterial growth, for example, in lipid transfer during cell envelope synthesis.


  • Organizational Affiliation

    School of Stomatology and Medicine, Foshan University, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cyclase/dehydrase
A, B
147Mycolicibacterium smegmatis MC2 155Mutation(s): 0 
Gene Names: MSMEI_0126
UniProt
Find proteins for I7FVL6 (Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155))
Explore I7FVL6 
Go to UniProtKB:  I7FVL6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupI7FVL6
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.210 
  • Space Group: P 62
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 109.76α = 90
b = 109.76β = 90
c = 56.5γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
Rosettaphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-03-21
    Type: Initial release
  • Version 1.1: 2018-05-09
    Changes: Data collection, Database references
  • Version 1.2: 2023-11-22
    Changes: Data collection, Database references, Refinement description