2acv
From Proteopedia
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Crystal Structure of Medicago truncatula UGT71G1
Overview
Glycosylation is a ubiquitous reaction controlling the bioactivity and, storage of plant natural products. Glycosylation of small molecules is, catalyzed by a superfamily of glycosyltransferases (GTs) in most plant, species studied to date. We present crystal structures of the UDP, flavonoid/triterpene GT UGT71G1 from Medicago truncatula bound to UDP or, UDP-glucose. The structures reveal the key residues involved in the, recognition of donor substrate and, by comparison with other GT, structures, suggest His-22 as the catalytic base and Asp-121 as a key, residue that may assist deprotonation of the acceptor by forming an, electron transfer chain with the catalytic base. Mutagenesis confirmed the, roles of these key residues in donor substrate binding and enzyme, activity. Our results provide an initial structural basis for, understanding the complex substrate specificity and regiospecificity, underlying the glycosylation of plant natural products and other small, molecules. This information will direct future attempts to engineer, bioactive compounds in crop plants to improve plant, animal, and human, health and to facilitate the rational design of GTs to improve the storage, and stability of novel engineered bioactive compounds.
About this Structure
2ACV is a Single protein structure of sequence from Medicago truncatula with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula., Shao H, He X, Achnine L, Blount JW, Dixon RA, Wang X, Plant Cell. 2005 Nov;17(11):3141-54. Epub 2005 Oct 7. PMID:16214900
Page seeded by OCA on Tue Jan 29 17:59:16 2008
Categories: Medicago truncatula | Single protein | Achnine, L. | Blount, J.W. | Dixon, R.A. | He, X. | Shao, H. | Wang, X. | UDP | Glycosyltransferase | Udp
