3CXP

Crystal structure of human glucosamine 6-phosphate N-acetyltransferase 1 mutant E156A

3CXP の概要

• エントリーDOI: 10.2210/pdb3cxp/pdb
• 関連するPDBエントリー: 3CXQ 3CXS
• 分子名称: Glucosamine 6-phosphate N-acetyltransferase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: gna1, acyltransferase, endosome, golgi apparatus, membrane, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus membrane; Peripheral membrane protein: Q96EK6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20753.53

構造登録者

Wang, J.,Liu, X.,Li, L.-F.,Su, X.-D. (登録日: 2008-04-25, 公開日: 2008-09-16, 最終更新日: 2023-11-01)

主引用文献

Wang, J.,Liu, X.,Liang, Y.-H.,Li, L.-F.,Su, X.-D.
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
Febs Lett., 582:2973-2978, 2008

PubMed Abstract: Glucosamine-6-phosphate (GlcN6P) N-acetyltransferase 1 (GNA1) is a key enzyme in the pathway toward biosynthesis of UDP-N-acetylglucosamine, an important donor substrate for N-linked glycosylation. GNA1 catalyzes the formation of N-acetylglucosamine-6-phosphate (GlcNAc6P) from acetyl-CoA (AcCoA) and the acceptor substrate GlcN6P. Here, we report crystal structures of human GNA1, including apo GNA1, the GNA1-GlcN6P complex and an E156A mutant. Our work showed that GlcN6P binds to GNA1 without the help of AcCoA binding. Structural analyses and mutagenesis studies have shed lights on the charge distribution in the GlcN6P binding pocket, and an important role for Glu156 in the substrate binding. Hence, these findings have broadened our knowledge of structural features required for the substrate affinity of GNA1.

PubMed: 18675810
DOI: 10.1016/j.febslet.2008.07.040

実験手法

X-RAY DIFFRACTION (2.01 Å)