5KOE

The structure of Arabidopsis thaliana FUT1 in complex with XXLG

5KOE の概要

• エントリーDOI: 10.2210/pdb5koe/pdb
• 分子名称: Galactoside 2-alpha-L-fucosyltransferase, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (8 entities in total)
• 機能のキーワード: acetyl transferase, xxlg, gt37, arabidopsis thaliana, cell adhesion
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein : Q9SWH5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 220451.98

構造登録者

Alahuhta, P.M.,Lunin, V.V. (登録日: 2016-06-30, 公開日: 2016-09-28, 最終更新日: 2020-07-29)

主引用文献

Urbanowicz, B.R.,Bharadwaj, V.S.,Alahuhta, M.,Pena, M.J.,Lunin, V.V.,Bomble, Y.J.,Wang, S.,Yang, J.Y.,Tuomivaara, S.T.,Himmel, M.E.,Moremen, K.W.,York, W.S.,Crowley, M.F.
Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism.
Plant J., 91:931-949, 2017

PubMed Abstract: The mechanistic underpinnings of the complex process of plant polysaccharide biosynthesis are poorly understood, largely because of the resistance of glycosyltransferase (GT) enzymes to structural characterization. In Arabidopsis thaliana, a glycosyl transferase family 37 (GT37) fucosyltransferase 1 (AtFUT1) catalyzes the regiospecific transfer of terminal 1,2-fucosyl residues to xyloglucan side chains - a key step in the biosynthesis of fucosylated sidechains of galactoxyloglucan. We unravel the mechanistic basis for fucosylation by AtFUT1 with a multipronged approach involving protein expression, X-ray crystallography, mutagenesis experiments and molecular simulations. Mammalian cell culture expressions enable the sufficient production of the enzyme for X-ray crystallography, which reveals the structural architecture of AtFUT1 in complex with bound donor and acceptor substrate analogs. The lack of an appropriately positioned active site residue as a catalytic base leads us to propose an atypical water-mediated fucosylation mechanism facilitated by an H-bonded network, which is corroborated by mutagenesis experiments as well as detailed atomistic simulations.

PubMed: 28670741
DOI: 10.1111/tpj.13628

実験手法

X-RAY DIFFRACTION (1.79 Å)