7EN5

The crystal structure of Escherichia coli MurR in complex with N-acetylglucosamine-6-phosphate

Summary for 7EN5

• Entry DOI: 10.2210/pdb7en5/pdb
• Descriptor: HTH-type transcriptional regulator MurR, 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total)
• Functional Keywords: regulator, n-acetylglucosamine-6-phosphate, sugar-binding, gene regulation
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 1
• Total formula weight: 21825.95

Authors

Zhang, Y.,Chen, W.,Ji, Q. (deposition date: 2021-04-16, release date: 2022-04-20, Last modification date: 2023-11-29)

Primary citation

Zhang, Y.,Chen, W.,Wu, D.,Liu, Y.,Wu, Z.,Li, J.,Zhang, S.Y.,Ji, Q.
Molecular basis for cell-wall recycling regulation by transcriptional repressor MurR in Escherichia coli.
Nucleic Acids Res., 50:5948-5960, 2022

PubMed Abstract: The cell-wall recycling process is important for bacterial survival in nutrient-limited conditions and, in certain cases, is directly involved in antibiotic resistance. In the sophisticated cell-wall recycling process in Escherichia coli, the transcriptional repressor MurR controls the expression of murP and murQ, which are involved in transporting and metabolizing N-acetylmuramic acid (MurNAc), generating N-acetylmuramic acid-6-phosphate (MurNAc-6-P) and N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Here, we report that both MurNAc-6-P and GlcNAc-6-P can bind to MurR and weaken the DNA binding ability of MurR. Structural characterizations of MurR in complex with MurNAc-6-P or GlcNAc-6-P as well as in the apo form revealed the detailed ligand recognition chemistries. Further studies showed that only MurNAc-6-P, but not GlcNAc-6-P, is capable of derepressing the expression of murQP controlled by MurR in cells and clarified the substrate specificity through the identification of key residues responsible for ligand binding in the complex structures. In summary, this study deciphered the molecular mechanism of the cell wall recycling process regulated by MurR in E. coli.

PubMed: 35640608
DOI: 10.1093/nar/gkac442

Experimental method

X-RAY DIFFRACTION (1.25 Å)