NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii

  • Non-ribosomal peptide synthetases (NRPSs) are large multienzyme machineries. They synthesize numerous important natural products starting from amino acids. For peptide synthesis functionally specialized NRPS modules interact in a defined manner. Individual modules are either located on a single or on multiple different polypeptide chains. The “peptide-antimicrobial-Xenorhabdus” (PAX) peptide producing NRPS PaxS from Xenorhabdus bacteria consists of the three proteins PaxA, PaxB and PaxC. Different docking domains (DDs) located at the N-termini of PaxB and PaxC and at the C-termini of PaxA and BaxB mediate specific non-covalent interactions between them. The N-terminal docking domains precede condensation domains while the C-terminal docking domains follow thiolation domains. The binding specificity of individual DDs is important for the correct assembly of multi-protein NRPS systems. In many multi-protein NRPS systems the docking domains are sufficient to mediate the necessary interactions between individual protein chains. However, it remains unclear if this is a general feature for all types of structurally different docking domains or if the neighboring domains in some cases support the function of the docking domains. Here, we report the 1H, 13C and 15 N NMR resonance assignments for a C-terminal di-domain construct containing a thiolation (T) domain followed by a C-terminal docking domain (CDD) from PaxA and for its binding partner – the N-terminal docking domain (NDD) from PaxB from the Gram-negative entomopathogenic bacterium Xenorhabdus cabanillasii JM26 in their free states and for a 1:1 complex formed by the two proteins. These NMR resonance assignments will facilitate further structural and dynamic studies of this protein complex.

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Author:Jonas WatzelORCiDGND, Sepas SarawiORCiD, Elke Duchardt-FernerORCiD, Helge Björn BodeORCiDGND, Jens WöhnertORCiDGND
Parent Title (English):Biomolecular NMR assignments
Publisher:Springer Netherlands
Place of publication:Dordrecht [u.a.]
Document Type:Article
Date of Publication (online):2021/03/05
Date of first Publication:2021/03/05
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2022/10/20
Tag:Docking domain; NMR assignments; Non-ribosomal peptide synthetase (NRPS); Peptide-antimicrobial-Xenorhabdus (PAX) peptide; Thiolation domain
Page Number:6
First Page:229
Last Page:234
Open Access funding enabled and organized by Projekt DEAL. The funding was supported by H2020 European Research Council (Grant No. 835108) and the LOEWE program of the state of Hesse (Grant No. MegaSyn Research Cluster).
Institutes:Biowissenschaften / Biowissenschaften
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0