4ZRA

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LPRG BINDING TO TRIACYLGLYCERIDE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Mycobacterial Metabolic Syndrome: LprG and Rv1410 Regulate Triacylglyceride Levels, Growth Rate and Virulence in Mycobacterium tuberculosis.

Martinot, A.J.Farrow, M.Bai, L.Layre, E.Cheng, T.Y.Tsai, J.H.Iqbal, J.Annand, J.W.Sullivan, Z.A.Hussain, M.M.Sacchettini, J.Moody, D.B.Seeliger, J.C.Rubin, E.J.

(2016) PLoS Pathog 12: e1005351-e1005351

  • DOI: https://doi.org/10.1371/journal.ppat.1005351
  • Primary Citation of Related Structures:  
    4ZRA

  • PubMed Abstract: 

    Mycobacterium tuberculosis (Mtb) mutants lacking rv1411c, which encodes the lipoprotein LprG, and rv1410c, which encodes a putative efflux pump, are dramatically attenuated for growth in mice. Here we show that loss of LprG-Rv1410 in Mtb leads to intracellular triacylglyceride (TAG) accumulation, and overexpression of the locus increases the levels of TAG in the culture medium, demonstrating a role of this locus in TAG transport. LprG binds TAG within a large hydrophobic cleft and is sufficient to transfer TAG from donor to acceptor membranes. Further, LprG-Rv1410 is critical for broadly regulating bacterial growth and metabolism in vitro during carbon restriction and in vivo during infection of mice. The growth defect in mice is due to disrupted bacterial metabolism and occurs independently of key immune regulators. The in vivo essentiality of this locus suggests that this export system and other regulators of metabolism should be considered as targets for novel therapeutics.


  • Organizational Affiliation

    Division of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts, United States of America.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lipoprotein LprGA,
B [auth C]
203Mycobacterium tuberculosis H37RvMutation(s): 0 
Gene Names: lprGlpp-27Rv1411cMTCY21B4.28c
UniProt
Find proteins for P9WK45 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WK45 
Go to UniProtKB:  P9WK45
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WK45
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
4RF
Query on 4RF

Download Ideal Coordinates CCD File 
C [auth A]Tripalmitoylglycerol
C51 H98 O6
PVNIQBQSYATKKL-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.83 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 95.677α = 90
b = 71.593β = 106.55
c = 61.894γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
REFMACrefinement
PDB_EXTRACTdata extraction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2016-02-10
    Type: Initial release
  • Version 1.1: 2016-02-17
    Changes: Derived calculations
  • Version 1.2: 2024-03-06
    Changes: Data collection, Database references, Derived calculations, Refinement description