2acw
From Proteopedia
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| - | [[Image:2acw.gif|left|200px]] | + | [[Image:2acw.gif|left|200px]] |
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| - | '''Crystal Structure of Medicago truncatula UGT71G1 complexed with UDP-glucose''' | + | {{Structure |
| + | |PDB= 2acw |SIZE=350|CAPTION= <scene name='initialview01'>2acw</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Medicago truncatula UGT71G1 complexed with UDP-glucose''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ACW is a [ | + | 2ACW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16214900 16214900] |
[[Category: Medicago truncatula]] | [[Category: Medicago truncatula]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: udp-glucose]] | [[Category: udp-glucose]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:48:08 2008'' |
Revision as of 13:48, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Medicago truncatula UGT71G1 complexed with UDP-glucose
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
2ACW is a Single protein structure of sequence from Medicago truncatula. 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 Thu Mar 20 15:48:08 2008
