2AM5

Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP

2AM5 の概要

• エントリーDOI: 10.2210/pdb2am5/pdb
• 関連するPDBエントリー: 1FO8 1FO9 1FOA
• 分子名称: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: transferase, n-acetylglucosaminyltransferase, glycosyltransferase, udp-glcnac, udp
• 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: 40644.74

構造登録者

Rini, J.M.,Gordon, R.D. (登録日: 2005-08-08, 公開日: 2006-06-27, 最終更新日: 2024-10-30)

主引用文献

Gordon, R.D.,Sivarajah, P.,Satkunarajah, M.,Ma, D.,Tarling, C.A.,Vizitiu, D.,Withers, S.G.,Rini, J.M.
X-ray Crystal Structures of Rabbit N-acetylglucosaminyltransferase I (GnT I) in Complex with Donor Substrate Analogues.
J.Mol.Biol., 360:67-79, 2006

PubMed Abstract: The Golgi-resident glycosyltransferase, UDP-N-acetyl-d-glucosamine:alpha-3-d-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnT I), initiates the conversion of high-mannose oligosaccharides to complex and hybrid structures in the biosynthesis of N-linked glycans. Reported here are the X-ray crystal structures of GnT I in complex with UDP-CH2-GlcNAc (a non-hydrolyzable C-glycosidic phosphonate), UDP-2-deoxy-2-fluoro-glucose, UDP-glucose and UDP. Collectively, these structures provide evidence for the importance of the GlcNAc moiety and its N-acetyl group in donor substrate binding, as well as insight into the role played by the flexible 318-330 loop in substrate binding and product release. In addition, the UDP-CH2-GlcNAc complex reveals a well-defined glycerol molecule poised for nucleophilic attack on the C1 atom of the donor substrate analogue. The position and orientation of this glycerol molecule have allowed us to model the binding of the Manalpha1,3Manbeta1 moiety of the acceptor substrate and, based on the model, to suggest a rationalization for the main determinants of GnT I acceptor specificity.

PubMed: 16769084
DOI: 10.1016/j.jmb.2006.04.058

実験手法

X-RAY DIFFRACTION (1.6 Å)