2VEZ

AfGNA1 crystal structure complexed with Acetyl-CoA and Glucose-6P gives new insights into catalysis

2VEZ の概要

• エントリーDOI: 10.2210/pdb2vez/pdb
• 関連するPDBエントリー: 2VXK
• 分子名称: PUTATIVE GLUCOSAMINE 6-PHOSPHATE ACETYLTRANSFERASE, ACETYL COENZYME *A, 6-O-phosphono-alpha-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: transferase, acyltransferase, glucosamine-6-phosphate n-acetyltransferase (gna1) udp-glcnac biosynthetic pathway
• 由来する生物種: ASPERGILLUS FUMIGATUS (SARTORYA FUMIGATA)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22290.79

構造登録者

Hurtado-Guerrero, R.,Raimi, O.,Shepherd, S.,van Aalten, D.M.F. (登録日: 2007-10-27, 公開日: 2009-03-10, 最終更新日: 2024-05-08)

主引用文献

Hurtado-Guerrero, R.,Raimi, O.,Shepherd, S.,Van Aalten, D.M.F.
Glucose-6-Phosphate as a Probe for the Glucosamine- 6-Phosphate N-Acetyltransferase Michaelis Complex.
FEBS Lett., 581:5597-, 2007

PubMed Abstract: Glucosamine-6-phosphate N-acetyltransferase (GNA1) catalyses the N-acetylation of d-glucosamine-6-phosphate (GlcN-6P), using acetyl-CoA as an acetyl donor. The product GlcNAc-6P is an intermediate in the biosynthesis UDP-GlcNAc. GNA1 is part of the GCN5-related acetyl transferase family (GNATs), which employ a wide range of acceptor substrates. GNA1 has been genetically validated as an antifungal drug target. Detailed knowledge of the Michaelis complex and trajectory towards the transition state would facilitate rational design of inhibitors of GNA1 and other GNAT enzymes. Using the pseudo-substrate glucose-6-phosphate (Glc-6P) as a probe with GNA1 crystals, we have trapped the first GNAT (pseudo-)Michaelis complex, providing direct evidence for the nucleophilic attack of the substrate amine, and giving insight into the protonation of the thiolate leaving group.

PubMed: 18005663
DOI: 10.1016/J.FEBSLET.2007.10.065

実験手法

X-RAY DIFFRACTION (1.45 Å)