6TRP
Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD
Summary for 6TRP
| Entry DOI | 10.2210/pdb6trp/pdb |
| NMR Information | BMRB: 34469 |
| Descriptor | Peptide synthetase XpsB,Peptide synthetase XpsB (1 entity in total) |
| Functional Keywords | protein, nrps, docking domains, communication-mediating domains, protein binding |
| Biological source | Xenorhabdus bovienii SS-2004 More |
| Total number of polymer chains | 1 |
| Total formula weight | 9841.62 |
| Authors | Watzel, J.,Hacker, C.,Duchardt-Ferner, E.,Bode, H.B.,Woehnert, J. (deposition date: 2019-12-19, release date: 2020-08-12, Last modification date: 2024-06-19) |
| Primary citation | Watzel, J.,Hacker, C.,Duchardt-Ferner, E.,Bode, H.B.,Wohnert, J. A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase fromXenorhabdus bovienii. Acs Chem.Biol., 15:982-989, 2020 Cited by PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) produce a wide variety of different natural products from amino acid precursors. In contrast to single protein NRPS, the NRPS of the bacterium producing the peptide-antimicrobial-Xenorhabdus (PAX) peptide consists of three individual proteins (PaxA/B/C), which interact with each other noncovalently in a linear fashion. The specific interactions between the three different proteins in this NRPS system are mediated by short C- and N-terminal docking domains (DDs). Here, we investigate the structural basis for the specific interaction between the DD from the protein PaxB and the DD from PaxC. The isolated DD peptides feature transient α-helical conformations in the absence of the respective DD partner. Isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR) titration experiments showed that the two isolated DDs bind to each other and form a structurally well-defined complex with a dissociation constant in the micromolar range as is typical for many DD interactions. Artificial linking of this DD pair via a flexible glycine-serine (GS) linker enabled us to solve the structure of the DD complex by NMR spectroscopy. In the complex, the two DDs interact with each other by forming a three helix bundle arranged in an overall coiled-coil motif. Key interacting residues were identified in mutagenesis experiments. Overall, our structure of the PaxB DD/PaxC DD complex represents an architecturally new type of DD interaction motif. PubMed: 32167274DOI: 10.1021/acschembio.9b01022 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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