7vyp

The structure of GdmN complex with the natural tetrahedral intermediate, carbamoylated derivative, and AMP

spinqualitylabelsall models 7vyp, resolution 2.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vyp is a 2 chain structure with sequence from Streptomyces hygroscopicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.88Å Ligands: 82Z, 8CW, AMP, CP, EDO, FE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q84G19_STRHY Publication Abstract from PubMed Iterative enzymes, which catalyze sequential reactions, have the potential to improve the atom economy and diversity of industrial enzymatic processes. Redesigning one-step enzymes to be iterative biocatalysts could further enhance these processes. Carbamoyltransferases (CTases) catalyze carbamoylation, an important modification for the bioactivity of many secondary metabolites with pharmaceutical applications. To generate an iterative CTase, we determine the X-ray structure of GdmN, a one-step CTase involved in ansamycin biosynthesis. GdmN forms a face-to-face homodimer through unusual C-terminal domains, a previously unknown functional form for CTases. Structural determination of GdmN complexed with multiple intermediates elucidates the carbamoylation process and identifies key binding residues within a spacious substrate-binding pocket. Further structural and computational analyses enable multi-site enzyme engineering, resulting in an iterative CTase with the capacity for successive 7-O and 3-O carbamoylations. Our findings reveal a subclade of the CTase family and exemplify the potential of protein engineering for generating iterative enzymes. Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies.,Wei J, Zhang X, Zhou Y, Cheng X, Lin Z, Tang M, Zheng J, Wang B, Kang Q, Bai L Nat Commun. 2022 Nov 3;13(1):6617. doi: 10.1038/s41467-022-34387-2. PMID:36329057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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