Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates

• Main Authors: Chen M.W., Lohkamp B., Schnell R., Lescar J., Schneider G.
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: Public Library of Science 2020
• Subjects: bacterial enzyme; flavine adenine nucleotide; nicotinamide; nicotinamide adenine dinucleotide phosphate; potassium ion; unclassified drug; uridine diphosphate n acetylglucosamine enolpyruvate reductase; bacterial protein; oxidoreductase; potassium; recombinant protein; UDP-N-acetylglucosamine-enolpyruvate; uridine diphosphate n acetylglucosamine; article; binding site; complex formation; controlled study; crystal structure; enzyme kinetics; enzyme localization; enzyme substrate; Escherichia coli; nonhuman; nucleotide sequence; protein conformation; protein structure; Pseudomonas aeruginosa; species comparison; amino acid sequence; analogs and derivatives; biosynthesis; chemistry; enzyme active site; enzyme specificity; enzymology; genetics; isolation and purification; metabolism; molecular dynamics; sequence alignment; X ray crystallography; Bacteria (microorganisms); Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Flavin-Adenine Dinucleotide; Molecular Dynamics Simulation; NADP; Oxidoreductases; Potassium; Recombinant Proteins; Sequence Alignment; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/166195
• Institution: National University of Singapore

10.1371/journal.pone.0066936