Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

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Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
Vv3GT is a GT-B enzyme. GT-B enzymes consists of two β/α/β Rossmann-like domains. The two domains are associated and face each other with the active-site lying between them. These domains are associated with the donor and acceptor substrate binding sites.
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The N- and C-terminal domain, linked by a flexible loop and α-helix with a hinge region. The C-terminal domain is highly conserved and binds the cosubstrate (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.
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The <scene name='69/692252/2c1z_rainbow/1'>N-terminal and C-terminal domain</scene>, linked by a flexible loop and α-helix with a hinge region. The C-terminal domain is highly conserved and binds the cosubstrate (e. g. UDP-Glc). On the other hand, the N-terminal domain is not conserved it binds the substrate and provides catalytically active amino acids.
{{Template:ColorKey_N52C3Rainbow}}
{{Template:ColorKey_N52C3Rainbow}}

Revision as of 14:31, 24 January 2015

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References

  1. Offen W, Martinez-Fleites C, Yang M, Kiat-Lim E, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ. Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO J. 2006 Mar 22;25(6):1396-405. Epub 2006 Feb 16. PMID:16482224

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Eyal Tamary, Raya Liberman, Michal Harel, Angel Herraez

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