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Titlel-2,3-Diaminopropionate Binding Mode of the SulM Adenylation Domain Limits Engineering Monobactam Analogue Biosynthesis with Larger Substrates.
Journal, issue, pagesJacs Au, Vol. 5, Page 1992-2003, Year 2025
Publish dateJan 27, 2025 (structure data deposition date)
AuthorsKahlert, L. / Patel, K.D. / Lichstrahl, M.S. / Li, R. / He, C. / Gulick, A.M. / Townsend, C.A.
External linksJacs Au / PubMed:40313847
MethodsX-ray diffraction
Resolution1.3 - 1.55 Å
Structure data

PDB-9n1u:
High-resolution crystal structure of 2,3-diamino propanoic acid bound adenylation domain (A3) from Sulfazecin nonribosomal peptide synthetase SulM
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-9n1v:
High-resolution crystal structure of methyl-2,3-diamino propanoic acid-AMS inhibitor bound adenylation domain (A3) from Sulfazecin nonribosomal peptide synthetase SulM
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-DPP:
DIAMINOPROPANOIC ACID

ChemComp-HOH:
WATER

PDB-1bva:
MANGANESE BINDING MUTANT IN CYTOCHROME C PEROXIDASE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • paraburkholderia acidicola (bacteria)
KeywordsLIGASE / Adenylation domain / NRPS / nonribosomal peptide synthetase / Sulfazecin

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