7KW2

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

7KW2 の概要

• エントリーDOI: 10.2210/pdb7kw2/pdb
• 分子名称: PCP-C didomain, 4'-PHOSPHOPANTETHEINE (3 entities in total)
• 機能のキーワード: nrps, c-domain, pcp-domain, biosynthetic protein
• 由来する生物種: Thermobifida fusca
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115492.31

構造登録者

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. (登録日: 2020-11-29, 公開日: 2021-03-24, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)