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Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea.
J Synchrotron Radiat. 2013 Nov; 20(Pt 6):894-8.JS

Abstract

Flowers of the butterfly pea (Clitoria ternatea) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in C. ternatea by UDP-glucose:anthocyanidin 3-O-glucosyltransferase (Ct3GT-A; AB185904). To elucidate the structure-function relationship of Ct3GT-A, recombinant Ct3GT-A was expressed in Escherichia coli and its tertiary structure was determined to 1.85 Å resolution by using X-ray crystallography. The structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like β/α/β domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of Ct3GT-A with that of the flavonoid glycosyltransferase VvGT1 from red grape (Vitis vinifera) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in Ct3GT-A, but certain residues of VvGT1 involved in binding kaempferol were found to be substituted in Ct3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes.

Authors+Show Affiliations

Quantum Beam Science Directorate, Japan Atomic Energy Agency, 2-4 Shirakata-Shirane, Tokai, Ibaraki 319-1195, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

24121335

Citation

Hiromoto, Takeshi, et al. "Crystal Structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase From Clitoria Ternatea." Journal of Synchrotron Radiation, vol. 20, no. Pt 6, 2013, pp. 894-8.
Hiromoto T, Honjo E, Tamada T, et al. Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea. J Synchrotron Radiat. 2013;20(Pt 6):894-8.
Hiromoto, T., Honjo, E., Tamada, T., Noda, N., Kazuma, K., Suzuki, M., & Kuroki, R. (2013). Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea. Journal of Synchrotron Radiation, 20(Pt 6), 894-8. https://doi.org/10.1107/S0909049513020712
Hiromoto T, et al. Crystal Structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase From Clitoria Ternatea. J Synchrotron Radiat. 2013;20(Pt 6):894-8. PubMed PMID: 24121335.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea. AU - Hiromoto,Takeshi, AU - Honjo,Eijiro, AU - Tamada,Taro, AU - Noda,Naonobu, AU - Kazuma,Kohei, AU - Suzuki,Masahiko, AU - Kuroki,Ryota, Y1 - 2013/09/29/ PY - 2013/05/24/received PY - 2013/07/25/accepted PY - 2013/10/15/entrez PY - 2013/10/15/pubmed PY - 2014/5/23/medline KW - anthocyanidin KW - crystal structure KW - glucosylation KW - glucosyltransferase SP - 894 EP - 8 JF - Journal of synchrotron radiation JO - J Synchrotron Radiat VL - 20 IS - Pt 6 N2 - Flowers of the butterfly pea (Clitoria ternatea) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in C. ternatea by UDP-glucose:anthocyanidin 3-O-glucosyltransferase (Ct3GT-A; AB185904). To elucidate the structure-function relationship of Ct3GT-A, recombinant Ct3GT-A was expressed in Escherichia coli and its tertiary structure was determined to 1.85 Å resolution by using X-ray crystallography. The structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like β/α/β domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of Ct3GT-A with that of the flavonoid glycosyltransferase VvGT1 from red grape (Vitis vinifera) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in Ct3GT-A, but certain residues of VvGT1 involved in binding kaempferol were found to be substituted in Ct3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes. SN - 1600-5775 UR - https://www.unboundmedicine.com/medline/citation/24121335/Crystal_structure_of_UDP_glucose:anthocyanidin_3_O_glucosyltransferase_from_Clitoria_ternatea_ L2 - http://scripts.iucr.org/cgi-bin/paper?S0909049513020712 DB - PRIME DP - Unbound Medicine ER -