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Structure paper

TitleStructure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity.
Journal, issue, pagesFEBS J., Vol. 284, Page 2981-2999, Year 2017
Publish dateFeb 27, 2017 (structure data deposition date)
AuthorsScaglione, A. / Fullone, M.R. / Montemiglio, L.C. / Parisi, G. / Zamparelli, C. / Vallone, B. / Savino, C. / Grgurina, I.
External linksFEBS J. / PubMed:28704585
MethodsX-ray diffraction
Resolution2.396 - 2.456 Å
Structure data

PDB-5n9w:
Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure
Method: X-RAY DIFFRACTION / Resolution: 2.456 Å

PDB-5n9x:
Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure
Method: X-RAY DIFFRACTION / Resolution: 2.396 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-THR:
THREONINE

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-8QN:
[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (2~{S},3~{R})-2-azanyl-3-oxidanyl-butanoate

Source
  • streptomyces sp. (bacteria)
KeywordsTRANSFERASE / adenylation domain / substrate specificity / non-ribosomal code / LIGASE / threonine adenylate

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