6trp | pdb_00006trp

Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD

spinqualitylabelsall models 6trp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6trp is a 1 chain structure with sequence from Xenorhabdus bovienii SS-2004. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D3V3G3_XENBS D3V3G2_XENBS Publication Abstract from PubMed 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 Xenorhabdus bovienii 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 ((C/N)DDs). Here, we investigate the structural basis for the specific interaction between the (C)DD from the protein PaxB and the (N)DD from PaxC. The isolated DD peptides feature transient alpha-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 (C)DD/PaxC (N)DD complex represents an architecturally new type of DD interaction motif. A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii.,Watzel J, Hacker C, Duchardt-Ferner E, Bode HB, Wohnert J ACS Chem Biol. 2020 Apr 17;15(4):982-989. doi: 10.1021/acschembio.9b01022. Epub, 2020 Mar 25. PMID:32167274 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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