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Abstract:
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 H-1, C-13 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 ((C)DD)
from PaxA and for its binding partner - the N-terminal docking domain
((DD)-D-N) 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.
