7RY6

Solution NMR structural bundle of the first cyclization domain from yersiniabactin synthetase (Cy1) impacted by dynamics

7RY6 の概要

• エントリーDOI: 10.2210/pdb7ry6/pdb
• NMR情報: BMRB: 30943
• 分子名称: HMWP2 nonribosomal peptide synthetase (1 entity in total)
• 機能のキーワード: heterocyclization, nonribosomal peptide synthetase, peptide bond formation, ligase
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51914.56

構造登録者

Kancherla, A.K.,Mishra, S.H.,Marincin, K.A.,Nerli, S.,Sgourakis, N.G.,Dowling, D.P.,Bouvignies, G.,Frueh, D.P. (登録日: 2021-08-24, 公開日: 2022-07-13, 最終更新日: 2024-05-15)

主引用文献

Mishra, S.H.,Kancherla, A.K.,Marincin, K.A.,Bouvignies, G.,Nerli, S.,Sgourakis, N.,Dowling, D.P.,Frueh, D.P.
Global protein dynamics as communication sensors in peptide synthetase domains.
Sci Adv, 8:eabn6549-eabn6549, 2022

PubMed Abstract: Biological activity is governed by the timely redistribution of molecular interactions, and static structural snapshots often appear insufficient to provide the molecular determinants that choreograph communication. This conundrum applies to multidomain enzymatic systems called nonribosomal peptide synthetases (NRPSs), which assemble simple substrates into complex metabolites, where a dynamic domain organization challenges rational design to produce new pharmaceuticals. Using a nuclear magnetic resonance (NMR) atomic-level readout of biochemical transformations, we demonstrate that global structural fluctuations help promote substrate-dependent communication and allosteric responses, and impeding these global dynamics by a point-site mutation hampers allostery and molecular recognition. Our results establish global structural dynamics as sensors of molecular events that can remodel domain interactions, and they provide new perspectives on mechanisms of allostery, protein communication, and NRPS synthesis.

PubMed: 35857508
DOI: 10.1126/sciadv.abn6549

実験手法

SOLUTION NMR