6vtz

Structure of a thiolation-reductase di-domain from an archaeal non-ribosomal peptide synthetase

spinqualitylabelsall models 6vtz, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vtz is a 1 chain structure with sequence from Methanobrevibacter ruminantium M1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D3E027_METRM Publication Abstract from PubMed Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes that produce a wide range of bio-active peptides such as siderophores, toxins, and antibacterial and insecticidal agents. NRPSs are dynamic proteins characterized by extensive inter-domain communications as a consequence of their assembly-line mode of synthesis. Hence, crystal structures of multi-domain fragments of NRPSs have aided in elucidating crucial inter-domain interactions that occur during different steps of the NRPS catalytic cycle. One crucial yet unexplored interaction is that between the reductase (R) domain and the peptide carrier protein (PCP) domain. Reductase domains are members of the short chain dehydrogenase/reductase (SDR) family and function as termination domains that catalyze the reductive release of the final peptide product from the terminal PCP domain of the NRPS. Here we report the crystal structure of an archaeal NRPS PCP-R di-domain construct. This is the first NRPS reductase domain structure to be determined together with the upstream PCP domain and is also the first structure of an archaeal NRPS to be reported. The structure reveals that a novel helix-turn-helix motif, found in NRPS reductase domains but not in other SDR family members, plays a major role in the interface between the PCP and reductase domains. The information derived from the described PCP-R interface will aid in gaining further mechanistic insights into the peptide termination reaction catalyzed by the reductase domain and may have implications in engineering NRPSs to synthesize novel peptide products. Structural characterization of a PCP-R di-domain from an archaeal non-ribosomal peptide synthetase reveals novel inter-domain interactions.,Deshpande S, Altermann E, Sarojini V, Lott JS, Lee TV J Biol Chem. 2021 Feb 18:100432. doi: 10.1016/j.jbc.2021.100432. PMID:33610550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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