5U3H
Solution structure of apo PCP1 from yersiniabactin synthetase
Summary for 5U3H
| Entry DOI | 10.2210/pdb5u3h/pdb |
| NMR Information | BMRB: 30205 |
| Descriptor | HMWP2 nonribosomal peptide synthetase (1 entity in total) |
| Functional Keywords | peptidyl carrier protein, nrps, ligase |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 1 |
| Total formula weight | 12353.52 |
| Authors | Harden, B.J.,Frueh, D.P. (deposition date: 2016-12-02, release date: 2017-02-08, Last modification date: 2024-05-15) |
| Primary citation | Harden, B.J.,Frueh, D.P. Molecular Cross-Talk between Nonribosomal Peptide Synthetase Carrier Proteins and Unstructured Linker Regions. Chembiochem, 18:629-632, 2017 Cited by PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) employ multiple domains separated by linker regions to incorporate substrates into natural products. During synthesis, substrates are covalently tethered to carrier proteins that translocate between catalytic partner domains. The molecular parameters that govern translocation and associated linker remodeling remain unknown. Here, we used NMR to characterize the structure, dynamics, and invisible states of a peptidyl carrier protein flanked by its linkers. We showed that the N-terminal linker stabilizes and interacts with the protein core while modulating dynamics at specific sites involved in post-translational modifications and/or domain interactions. The results detail the molecular communication between peptidyl carrier proteins and their linkers and could guide efforts in engineering NRPSs to obtain new pharmaceuticals. PubMed: 28120469DOI: 10.1002/cbic.201700030 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
