25RW image
Deposition Date 2026-04-16
Release Date 2026-09-30
Last Version Date 2026-09-30
Entry Detail
PDB ID:
25RW
Title:
Peptidoglycan and lipopolysaccharide biosynthesis enzymes with inhibitor
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.35 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:UDP-N-acetylglucosamine 1-car
Gene (Uniprot):lpxC, murA
Chain IDs:A, B
Chain Length:0
Number of Molecules:2
Biological Source:Pseudomonas aeruginosa PAO1
Ligand Molecules
Primary Citation
Structure of the MurA-LpxC enzyme complex in modulating peptidoglycan and lipopolysaccharide biosynthesis.
J.Struct.Biol. ? 108374 108374 (2026)
PMID: 42762934 DOI: 10.1016/j.jsb.2026.108374

Abstact

Coordination of peptidoglycan and lipopolysaccharide biosynthesis is essential for maintaining Gram-negative cell envelope homeostasis. Two enzymes, MurA and LpxC, catalyze the first committed steps in peptidoglycan and lipopolysaccharide biosynthesis, respectively. Here, we determined cryo-electron microscopy (cryo-EM) structures of the Pseudomonas aeruginosa MurA-LpxC complex in the absence and presence of the LpxC inhibitor CHIR-090, providing molecular insights into complex formation. Structure-guided mutagenesis of MurA, together with in vitro pull-down assays, identified residues crucial for complex formation. We show that MurA G58 favors, but is not sufficient for complex formation, as substitution of this residue to mimic Escherichia coli MurA (G58S) weakens the interaction. Together, our study advances our structural understanding of how two biosynthesis pathways for peptidoglycan and lipopolysaccharide are coordinated to maintain a synergistic and balanced cell envelope.

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Primary Citation of related structures
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