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Structure paper

TitleThe specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.
Journal, issue, pagesSci Adv, Vol. 10, Page eadm9404-eadm9404, Year 2024
Publish dateSep 26, 2023 (structure data deposition date)
AuthorsKaranth, M.N. / Kirkpatrick, J.P. / Krausze, J. / Schmelz, S. / Scrima, A. / Carlomagno, T.
External linksSci Adv / PubMed:38896613
MethodsX-ray diffraction / NMR (solution)
Resolution1.65 - 2.3 Å
Structure data

PDB-8qnf:
Crystal structure of the Condensation domain TomBC from the Tomaymycin non-ribosomal peptide synthetase
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-8qpy:
Solution NMR structure of the peptidyl carrier domain TomAPCP from the Tomaymycin non-ribosomal peptide synthetase
Method: SOLUTION NMR

PDB-8qrx:
Solution NMR structure of the peptidyl carrier domain TomAPCP from the Tomaymycin non-ribosomal peptide synthetase in its substrate-loaded state
Method: SOLUTION NMR

PDB-8qsx:
Solution NMR structure of the novel adaptor domain TomBN91 from the Tomaymycin non-ribosomal peptide synthetase
Method: SOLUTION NMR

PDB-8rz6:
SeMet derivative structure of the condensation domain TomBC from the Tomaymycin non-ribosomal peptide synthetase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-FMT:
FORMIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • streptomyces regensis (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / Non-ribosomal peptide synthetase / Tomaymycin / Condensation / PCP / phosphopantetheine / Donor / NRPS / Peptidyl carrier protein / loaded / substrate-loaded / novel protein / Adaptor protein

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