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Crystal structure of UDP-glucose: anthocyanidin 3-${it O}$- glucosyltransferase from ${it Clitoria ternatea}$

Hiromoto, Takeshi; Honjo, Eijiro*; Tamada, Taro; Kuroki, Ryota

UDP-glucose: anthocyanidin 3-${it O}$-glucosyltransferase from ${it Clitoria ternatea}$ (${it Ct}$3GT-A; AB185904) is an enzyme that catalyses glucosyl transfer from UDP-glucose to anthocyanidins such as delphinidin, which is the first step of ternatin biosynthesis (Kogawa ${it et al}$., 2007). The recombinant wild-type enzyme was expressed in ${it E. coli}$ cells, purified to homogeneity and crystallized. The X-ray diffraction data set was collected at PF-BL6A using a crystal with a size of 0.05 $$times$$ 0.05 $$times$$ 0.5 mm, which belongs to the space group ${it P}$2$$_{1}$$ with cell dimensions of ${it a}$ = 50.2 ${AA}$, ${it b}$ = 55.2 ${AA}$, ${it c}$ = 86.2 ${AA}$ and $$beta$$ = 105.1 $$^{circ}$$. The initial phase was solved by MR using the coordinates of a homologous glucosyltransferase ${it Vv}$GT1 from ${it Vitis vinifera}$ (PDB ID: 2C1Z) as a search model. The overall structure of ${it Ct}$3GT-A shows a typical GT-B fold comprising two Rossmann-like $$beta$$/$$alpha$$/$$beta$$ domains. The putative binding sites for UDP-glucose and delphinidin are located in a deep cleft between the N- and C-terminal domains. Structural homology searches by Dali server indicated that ${it Ct}$3GT-A is similar to the other plant glucosyltransferases ${it Vv}$GT1 and UGT78G1 from ${it Medicago truncatula}$ with the RMS deviations of 1.9 ${AA}$ (for 432 C$$alpha$$ atoms) and 2.0 ${AA}$ (for 437 C$$alpha$$ atoms), respectively.

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