TY  - JOUR
A1  - Watzel, Jonas
A1  - Sarawi, Sepas
A1  - Duchardt-Ferner, Elke
A1  - Bode, Helge Björn
A1  - Wöhnert, Jens
T1  - NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
T2  - Biomolecular NMR assignments
N2  - 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.
KW  - NMR assignments
KW  - Peptide-antimicrobial-Xenorhabdus (PAX) peptide
KW  - Non-ribosomal peptide synthetase (NRPS)
KW  - Docking domain
KW  - Thiolation domain
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63743
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-637439
SN  - 1874-270X
N1  - 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).
VL  - 15
IS  - 1
SP  - 229
EP  - 234
PB  - Springer Netherlands
CY  - Dordrecht [u.a.]
ER  -