9ir5

Crystal structure of apo-form UDP-N-acetylmuramic Acid L-alanine ligase (MurC) from Roseburia faecis

spinqualitylabelsall models 9ir5, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ir5 is a 1 chain structure with sequence from Roseburia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.36Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M6X1Q9_9FIRM Cell wall formation.[HAMAP-Rule:MF_00046] Publication Abstract from PubMed Developing selective labeling probes for specific bacterial taxa can not only facilitate the study of target bacteria but also deepen our understanding of the microbial diversity at structural and molecular levels. The availability of such probes, however, remains very limited. In this study, by exploiting the variation of amino acids in peptidoglycan stem peptide, we designed a fluorescent L-amino acid probe and found that it can selectively target the family Lachnospiraceae (a major Gram-positive family in murine gut microbiome) in vivo. The following in vitro test using two Roseburia species belonging to this family validated labeling by the probe. We then discovered that the labeling site is the first amino acid (L-alanine in most bacteria), which links the stem peptide with N-acetylmuramic acid, a process catalyzed by a highly conserved enzyme MurC. An enzyme assay of Roseburia MurC demonstrated its ability to conjugate a fluorescent L-amino acid and other non-L-Ala amino acids to UDP-N-acetylmuramic acid. Subsequent X-ray crystallography analysis uncovered a substantially enlarged inner space in this enzyme, which can partially explain its tolerance to these atypical substrates. The resulting unusual peptidoglycan structures lead to significantly reduced activation of the NOD immune receptors, suggesting a new mechanism for the host to accommodate these highly abundant commensals. Unusual MurC Ligase and Peptidoglycan Discovered in Lachnospiraceae Using a Fluorescent L-Amino Acid Based Selective Labeling Probe.,Du Y, Wang Y, Yang M, Lin L, Zhang J, Huang Z, Liu C, Liu S, Ma J, Yang C, Wang W Angew Chem Int Ed Engl. 2025 Mar 28:e202503049. doi: 10.1002/anie.202503049. PMID:40152026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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