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8QZG

1,3 L,D-transpeptidase from Gluconobacter oxydans

Summary for 8QZG
Entry DOI10.2210/pdb8qzg/pdb
DescriptorYkuD domain-containing protein, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
Functional Keywordstranspeptidase, peptidoglycan, gluconobacter oxydans, cell wall, antibiotics resistance, lipoprotein, transferase
Biological sourceGluconobacter oxydans
Total number of polymer chains1
Total formula weight36116.64
Authors
ter Beek, J.,Berntsson, R.P. (deposition date: 2023-10-27, release date: 2023-11-08, Last modification date: 2024-03-06)
Primary citationEspaillat, A.,Alvarez, L.,Torrens, G.,Ter Beek, J.,Miguel-Ruano, V.,Irazoki, O.,Gago, F.,Hermoso, J.A.,Berntsson, R.P.,Cava, F.
A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria.
Nat Commun, 15:1343-1343, 2024
Cited by
PubMed Abstract: The bacterial cell-wall peptidoglycan is made of glycan strands crosslinked by short peptide stems. Crosslinks are catalyzed by DD-transpeptidases (4,3-crosslinks) and LD-transpeptidases (3,3-crosslinks). However, recent research on non-model species has revealed novel crosslink types, suggesting the existence of uncharacterized enzymes. Here, we identify an LD-transpeptidase, LDT, that generates 1,3-crosslinks in the acetic-acid bacterium Gluconobacter oxydans. LDT-like proteins are found in Alpha- and Betaproteobacteria lacking LD3,3-transpeptidases. In contrast with the strict specificity of typical LD- and DD-transpeptidases, LDT can use non-terminal amino acid moieties for crosslinking. A high-resolution crystal structure of LDT reveals unique features when compared to LD3,3-transpeptidases, including a proline-rich region that appears to limit substrate access, and a cavity accommodating both glycan chain and peptide stem from donor muropeptides. Finally, we show that DD-crosslink turnover is involved in supplying the necessary substrate for LD1,3-transpeptidation. This phenomenon underscores the interplay between distinct crosslinking mechanisms in maintaining cell wall integrity in G. oxydans.
PubMed: 38351082
DOI: 10.1038/s41467-024-45620-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.73 Å)
Structure validation

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