1FO8

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

1FO8 の概要

• エントリーDOI: 10.2210/pdb1fo8/pdb
• 関連するPDBエントリー: 1FO9 1FOA
• 分子名称: ALPHA-1,3-MANNOSYL-GLYCOPROTEIN BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE, METHYL MERCURY ION (3 entities in total)
• 機能のキーワード: methylmercury derivative, alpha-1, 3-mannosyl-glycoprotein beta-1, 2-n-acetylglucosaminyltransferase, n-acetylglucosaminyltransferase i, transferase
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Golgi apparatus membrane; Single-pass type II membrane protein: P27115
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40053.95

構造登録者

Unligil, U.M.,Zhou, S.,Yuwaraj, S.,Sarkar, M.,Schachter, H.,Rini, J.M. (登録日: 2000-08-26, 公開日: 2001-04-25, 最終更新日: 2024-10-23)

主引用文献

Unligil, U.M.,Zhou, S.,Yuwaraj, S.,Sarkar, M.,Schachter, H.,Rini, J.M.
X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily.
EMBO J., 19:5269-5280, 2000

PubMed Abstract: N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.

PubMed: 11032794
DOI: 10.1093/emboj/19.20.5269

実験手法

X-RAY DIFFRACTION (1.4 Å)