3TSA

Spinosyn Rhamnosyltransferase SpnG

3TSA の概要

• エントリーDOI: 10.2210/pdb3tsa/pdb
• 分子名称: NDP-rhamnosyltransferase, MAGNESIUM ION, alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, transferase
• 由来する生物種: Saccharopolyspora spinosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82916.64

構造登録者

Isiorho, E.A.,Liu, H.-W.,Keatinge-Clay, A.T. (登録日: 2011-09-12, 公開日: 2012-02-15, 最終更新日: 2023-09-13)

主引用文献

Isiorho, E.A.,Liu, H.W.,Keatinge-Clay, A.T.
Structural Studies of the Spinosyn Rhamnosyltransferase, SpnG.
Biochemistry, 51:1213-1222, 2012

PubMed Abstract: Spinosyns A and D (spinosad), like many other complex polyketides, are tailored near the end of their biosyntheses through the addition of sugars. SpnG, which catalyzes their 9-OH rhamnosylation, is also capable of adding other monosaccharides to the spinosyn aglycone (AGL) from TDP-sugars; however, the substitution of UDP-D-glucose for TDP-D-glucose as the donor substrate is known to result in a >60000-fold reduction in k(cat). Here, we report the structure of SpnG at 1.65 Å resolution, SpnG bound to TDP at 1.86 Å resolution, and SpnG bound to AGL at 1.70 Å resolution. The SpnG-TDP complex reveals how SpnG employs N202 to discriminate between TDP- and UDP-sugars. A conformational change of several residues in the active site is promoted by the binding of TDP. The SpnG-AGL complex shows that the binding of AGL is mediated via hydrophobic interactions and that H13, the potential catalytic base, is within 3 Å of the nucleophilic 9-OH group of AGL. A model for the Michaelis complex was constructed to reveal the features that allow SpnG to transfer diverse sugars; it also revealed that the rhamnosyl moiety is in a skew-boat conformation during the transfer reaction.

PubMed: 22283226
DOI: 10.1021/bi201860q

実験手法

X-RAY DIFFRACTION (1.7 Å)