Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)

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The plant UGTs are characterized by sharing a highly conserved 44 amino acid motif referred to as the
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). Amino acids of the PSPG motif provide most of the interactions with the sugar donor molecule.
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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. 10 highly conserved residues of the 44 amino acid PSPG motif are observed to directly interact with the UDP-sugar. In Vv3GT the PSPG motif begins with Pro 334 and ends with Gln 375.
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.
== Quiz ==
== Quiz ==
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Revision as of 08:36, 25 January 2015

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References

1. Offen W, Martinez-Fleites C, Yang M, Lim EK, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO 25: 1396-1405.

2. Osmani SA, Bak S, Møller BL (2009) Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70: 325-347.

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