8je4

Crystal structure of LimF prenyltransferase (H239G/W273T mutant) bound with the thiodiphosphate moiety of farnesyl S-thiolodiphosphate (FSPP)

spinqualitylabelsall models 8je4, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8je4 is a 2 chain structure with sequence from Limnothrix sp. CACIAM 69d. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.19Å Ligands: MG, PIS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A372DCN7_9CYAN Publication Abstract from PubMed Prenyltransferases in cyanobactin biosynthesis are of growing interest as peptide alkylation biocatalysts, but their prenylation modes characterized so far have been limited to dimethylallylation (C5) or geranylation (C10). Here we engaged in structure-guided engineering of the prenyl-binding pocket of a His-C2-geranyltransferase LimF to modulate its prenylation mode. Contraction of the pocket by a single mutation led to a His-C2-dimethylallyltransferase. More importantly, pocket expansion by a double mutation successfully repurposed LimF for farnesylation (C15), which is an unprecedented mode in this family. Furthermore, the obtained knowledge of the essential residues to construct the farnesyl-binding pocket has allowed for rational design of a Tyr-O-farnesyltransferase by a triple mutation of a Tyr-O-dimethylallyltransferase PagF. These results provide an approach to manipulate the prenyl specificity of cyanobactin prenyltransferases, broadening the chemical space covered by this class of enzymes and expanding the toolbox of peptide alkylation biocatalysts. Switching Prenyl Donor Specificities of Cyanobactin Prenyltransferases.,Zhang Y, Hamada K, Satake M, Sengoku T, Goto Y, Suga H J Am Chem Soc. 2023 Nov 8;145(44):23893-23898. doi: 10.1021/jacs.3c07373. Epub , 2023 Oct 25. PMID:37877712 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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