7KW2

Non-ribosomal didomain (holo-PCP-C) acceptor bound state, R2577G

Summary for 7KW2

• Entry DOI: 10.2210/pdb7kw2/pdb
• Descriptor: PCP-C didomain, 4'-PHOSPHOPANTETHEINE (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: 115492.31

Authors

Izore, T.,Ho, Y.T.C.,Kaczmarski, J.A.,Gavriilidou, A.,Chow, K.H.,Steer, D.,Goode, R.J.A.,Schittenhelm, R.B.,Tailhades, J.,Tosin, M.,Challis, G.L.,Krenske, E.H.,Ziemert, N.,Jackson, C.J.,Cryle, M.J. (deposition date: 2020-11-29, release date: 2021-03-24, Last modification date: 2024-04-03)

Primary citation

Izore, T.,Candace Ho, Y.T.,Kaczmarski, J.A.,Gavriilidou, A.,Chow, K.H.,Steer, D.L.,Goode, R.J.A.,Schittenhelm, R.B.,Tailhades, J.,Tosin, M.,Challis, G.L.,Krenske, E.H.,Ziemert, N.,Jackson, C.J.,Cryle, M.J.
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.
Nat Commun, 12:2511-2511, 2021

PubMed Abstract: Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains.

PubMed: 33947858
DOI: 10.1038/s41467-021-22623-0

Experimental method

X-RAY DIFFRACTION (2 Å)