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Structure paper

TitleThe structural basis of substrate selectivity of the acinetobactin biosynthetic adenylation domain, BasE.
Journal, issue, pagesJ. Biol. Chem., Vol. 301, Page 108413-108413, Year 2025
Publish dateJan 21, 2025 (structure data deposition date)
AuthorsAhmed, S.F. / Gulick, A.M.
External linksJ. Biol. Chem. / PubMed:40096888
MethodsX-ray diffraction
Resolution2.07 - 2.53 Å
Structure data

PDB-9my5:
Structure of the BasE mutant V336A, an NRPS adenylation domain in the acinetobactin biosynthetic pathway bound to 4-methyl salicylic Acid
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

PDB-9my6:
Structure of the BasE double mutant V336A/S247C, an NRPS adenylation domain in the acinetobactin biosynthetic pathway bound to 4-fluoro salicylic Acid
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-9my7:
Structure of the BasE mutant V336G, an NRPS adenylation domain in the acinetobactin biosynthetic pathway bound to 4-amino salicylic acid
Method: X-RAY DIFFRACTION / Resolution: 2.53 Å

Chemicals

PDB-1bub:
DETERMINATION OF INTERNUCLEAR ANGLES OF DNA USING PARAMAGNETIC ASSISTED MAGNETIC ALIGNMENT

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER


ChemComp, No image

ChemComp-OOI:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-BHA:
2-HYDROXY-4-AMINOBENZOIC ACID / medication, antibiotic*YM

Source
  • acinetobacter baumannii (bacteria)
KeywordsLIGASE / NRPS / Adenylation Domain / Nonribosomal peptide siderophore / acinetobactin / synthetase

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