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Structure paper

TitleStructural basis of keto acid utilization in nonribosomal depsipeptide synthesis.
Journal, issue, pagesNat. Chem. Biol., Vol. 16, Page 493-496, Year 2020
Publish dateOct 8, 2019 (structure data deposition date)
AuthorsAlonzo, D.A. / Chiche-Lapierre, C. / Tarry, M.J. / Wang, J. / Schmeing, T.M.
External linksNat. Chem. Biol. / PubMed:32066969
MethodsX-ray diffraction
Resolution2.3 - 3.4 Å
Structure data

PDB-6ulw:
Adenylation, ketoreductase, and pseudo Asub multidomain structure of a keto acid-selecting NRPS module
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-6ulx:
Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P43212
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-6uly:
Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P212121
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-6ulz:
Adenylation domain of the initiation module of LgrA mutant P483M
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-QA7:
5'-O-{(S)-hydroxy[(4-methyl-2-oxopentanoyl)oxy]phosphoryl}adenosine

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-FMT:
FORMIC ACID

ChemComp-APC:
DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER / AMP-CPP, energy-carrying molecule analogue*YM

ChemComp-KIV:
3-METHYL-2-OXOBUTANOIC ACID

Source
  • bacillus stratosphericus lama 585 (bacteria)
  • brevibacillus parabrevis (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / NRPS / Nonribosomal peptide synthetase / non-ribosomal peptide synthetase / adenylation / adenylation domain / depsipeptide / cereulide / valinomycin / natural product / adenylate / keto acid / ketoacid / ketoreductase / short chain dehydrogenase

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