8FX6
Non-ribosomal PCP-C didomain (amide stabilised leucine) acceptor bound state
Summary for 8FX6
Entry DOI | 10.2210/pdb8fx6/pdb |
Descriptor | PCP-C didomain, N-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]-L-leucinamide (3 entities in total) |
Functional Keywords | nrps, c-domain, pcp-domain, biosynthetic protein |
Biological source | Thermobifida fusca |
Total number of polymer chains | 2 |
Total formula weight | 114487.25 |
Authors | Ho, Y.T.C.,Cryle, M.J. (deposition date: 2023-01-24, release date: 2023-06-21, Last modification date: 2024-11-13) |
Primary citation | Ho, Y.T.C.,Kaczmarski, J.A.,Tailhades, J.,Izore, T.,Steer, D.L.,Schittenhelm, R.B.,Tosin, M.,Jackson, C.J.,Cryle, M.J. Not always an innocent bystander: the impact of stabilised phosphopantetheine moieties when studying nonribosomal peptide biosynthesis. Chem.Commun.(Camb.), 59:8234-8237, 2023 Cited by PubMed Abstract: Nonribosomal peptide synthetases produce many important peptide natural products and are centred around carrier proteins (CPs) that deliver intermediates to various catalytic domains. We show that the replacement of CP substrate thioesters by stabilised ester analogues leads to active condensation domain complexes, whereas amide stabilisation generates non-functional complexes. PubMed: 37310188DOI: 10.1039/d3cc01578e PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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