5INJ

Crystal Structure of Prenyltransferase PriB Ternary Complex with L-Tryptophan and Dimethylallyl thiolodiphosphate (DMSPP)

Summary for 5INJ

• Entry DOI: 10.2210/pdb5inj/pdb
• Descriptor: Prenyltransferase, TRYPTOPHAN, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: prenyltransferase, tryptophan, dmspp, indole-pt, abba family, pt fold, structural genomics, psi-2, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, transferase
• Biological source: Streptomyces sp. RM-5-8
• Total number of polymer chains: 1
• Total formula weight: 43989.22

Authors

Cao, H.,Elshahawi, S.,Benach, J.,Wasserman, S.R.,Morisco, L.L.,Koss, J.W.,Thorson, J.S.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2016-03-07, release date: 2016-05-11, Last modification date: 2024-03-06)

Primary citation

Elshahawi, S.I.,Cao, H.,Shaaban, K.A.,Ponomareva, L.V.,Subramanian, T.,Farman, M.L.,Spielmann, H.P.,Phillips, G.N.,Thorson, J.S.,Singh, S.
Structure and specificity of a permissive bacterial C-prenyltransferase.
Nat. Chem. Biol., 13:366-368, 2017

PubMed Abstract: This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.

PubMed: 28166207
DOI: 10.1038/nchembio.2285

Experimental method

X-RAY DIFFRACTION (1.4 Å)