3S2U

Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.23 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.214 

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This is version 1.3 of the entry. See complete history. 


Literature

Crystal Structure of the Pseudomonas aeruginosa MurG: UDP-GlcNAc Substrate Complex.

Brown, K., Vial, S.C., Dedi, N., Westcott, J., Scally, S., Bugg, T.D., Charlton, P.A., Cheetham, G.M.

(2013) Protein Pept Lett 20: 1002-1008

  • DOI: https://doi.org/10.2174/0929866511320090006
  • Primary Citation of Related Structures:  
    3S2U

  • PubMed Abstract: 

    MurG is an essential bacterial glycosyltransferase enzyme in Pseudomonas aeruginosa performing one of the key membrane steps of peptidoglycan synthesis catalyzing the transfer of N-acetyl glucosamine (GlcNAc) from its donor substrate, UDP-GlcNAc, to the acceptor substrate Lipid I. We have solved the crystal structure of the complex between Pseudomonas aeruginosa MurG and UDP-GlcNAc and compared it with the previously solved complex from E. coli. The structure reveals a large-scale conformational change in the relative orientations of the N- and C-terminal domains, which has the effect of widening the cofactor binding site and displacing the UDP-GlcNAc donor. These results suggest new opportunities to design potent inhibitors of peptidoglycan biosynthesis.

    • Organizational Affiliation: 

    Vertex Pharmaceuticals (Europe) Ltd, 88 Milton Park, Abingdon, Oxfordshire, OX14 4RY, UK. kieron_brown@vrtx.com


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase365Pseudomonas aeruginosa PAO1Mutation(s): 0 
Gene Names: murG, PA4412
EC: 2.4.1.227
Membrane Entity: Yes 
UniProt
Find proteins for Q9HW01 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
Explore Q9HW01 
Go to UniProtKB:  Q9HW01
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9HW01
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
UD1
Query on UD1
Download Ideal Coordinates CCD File 
B [auth A]URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
C17 H27 N3 O17 P2
LFTYTUAZOPRMMI-CFRASDGPSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.23 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.214 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.93α = 90
b = 49.93β = 90
c = 278.62γ = 90
Software Package:
Software NamePurpose
DNAdata collection
AMoREphasing
CNSrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-09-26
    Type: Initial release
  • Version 1.1: 2013-05-08
    Changes: Database references
  • Version 1.2: 2013-08-14
    Changes: Database references
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references, Derived calculations