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.
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Plant glycosyltransferases assume one of two folds, GT-A or GT-B. 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 <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.
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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 linker could be important for sugar donor binding. This linker region holds the UDP-sugar donor next to the C-terminal PSPG motif. The C-terminal domain is highly conserved and binds the UDP sugar donor (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 plant UGTs are characterized by sharing a highly conserved motif referred to as the
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The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
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<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif).
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<scene name='69/692252/2c1z_pspg/1'>PSPG</scene> motif (Plant Secondary Product Glycosyltransferase motif). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule.
Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.
Three conserved motifs involved in sugar binding are present in Vv3GT. The first, a <scene name='60/607848/2c1z_loop_n5_label/1'>loopN5</scene> motif (Thr 141; Ala 142) involved in sugar binding. The second, a <scene name='69/692252/2c1z_wns_label/1'>WNS</scene> (Trp 354; Asn 355; Ser 356) motif residues are involved in binding UDP phosphates. The third, <scene name='69/692252/2c1z_d_eq_label/1'>D/EQ</scene> motif residues also involved in sugar binding (Asp 374; Gln 375). The WNS and D/EQ motifs are part of the highly conserved PSPG region.

Revision as of 08:21, 25 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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