6u1r

SxtG an amidinotransferase from the Microseira wollei in Saxitoxin biosynthetic pathway

spinqualitylabelsall models 6u1r, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6u1r is a 2 chain structure with sequence from Microseira wollei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.792Å Ligands: FMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C3RVP0_9CYAN Publication Abstract from PubMed Secondary metabolites are assembled by enzymes that often perform reactions with high selectivity and specificity. Many of these enzymes also tolerate variations in substrate structure, exhibiting promiscuity that enables various applications of a given biocatalyst. However, initial enzyme characterization studies frequently do not explore beyond the native substrates. This limited assessment of substrate scope contributes to the difficulty of identifying appropriate enzymes for specific synthetic applications. Here, we report the natural function of cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins, and demonstrate its ability to modify a breadth of non-native substrates. In addition, we report the first X-ray crystal structure of SxtG, which provides rationale for this enzyme's substrate scope. Taken together, these data confirm the function of SxtG and exemplify its potential utility in biocatalytic synthesis. Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase.,Lukowski AL, Mallik L, Hinze ME, Carlson BM, Ellinwood DC, Pyser JB, Koutmos M, Narayan ARH ACS Chem Biol. 2020 Feb 14. doi: 10.1021/acschembio.9b00964. PMID:32058687 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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