7RY6
Solution NMR structural bundle of the first cyclization domain from yersiniabactin synthetase (Cy1) impacted by dynamics
Summary for 7RY6
| Entry DOI | 10.2210/pdb7ry6/pdb |
| NMR Information | BMRB: 30943 |
| Descriptor | HMWP2 nonribosomal peptide synthetase (1 entity in total) |
| Functional Keywords | heterocyclization, nonribosomal peptide synthetase, peptide bond formation, ligase |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 1 |
| Total formula weight | 51914.56 |
| Authors | Kancherla, A.K.,Mishra, S.H.,Marincin, K.A.,Nerli, S.,Sgourakis, N.G.,Dowling, D.P.,Bouvignies, G.,Frueh, D.P. (deposition date: 2021-08-24, release date: 2022-07-13, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 35857508DOI: 10.1126/sciadv.abn6549 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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