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Structure paper

TitleRadical S-Adenosyl-l-methionine Tryptophan Lyase (NosL): How the Protein Controls the Carboxyl Radical •CO2-Migration.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 140, Page 16661-16668, Year 2018
Publish dateOct 4, 2018 (structure data deposition date)
AuthorsAmara, P. / Mouesca, J.M. / Bella, M. / Martin, L. / Saragaglia, C. / Gambarelli, S. / Nicolet, Y.
External linksJ. Am. Chem. Soc. / PubMed:30418774
MethodsX-ray diffraction
Resolution1.45 - 2 Å
Structure data

PDB-6htk:
X-ray structure of the tryptophan lyase NosL in complex with (R)-(+)-indoline-2-carboxylate
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6htm:
X-ray structure of the tryptophan lyase NosL in complex with bound tryptamin
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6hto:
Tryptophan lyase 'empty state'
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-GOL:
GLYCEROL

ChemComp-BR:
BROMIDE ION

ChemComp-NA:
Unknown entry

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-MET:
METHIONINE

ChemComp-5AD:
5'-DEOXYADENOSINE

ChemComp-ICB:
1H-indole-2-carboxylic acid

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-TSS:
2-(1H-INDOL-3-YL)ETHANAMINE

ChemComp-CL:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • streptomyces actuosus (bacteria)
KeywordsANTIBIOTIC / Radical SAM / FeS cluster / Nosiheptide / tryptophan lyase / NosL

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