1I1D

CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P

1I1D の概要

• エントリーDOI: 10.2210/pdb1i1d/pdb
• 関連するPDBエントリー: 1I12 1I21
• 分子名称: GLUCOSAMINE-PHOSPHATE N-ACETYLTRANSFERASE, 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, COENZYME A, ... (5 entities in total)
• 機能のキーワード: alpha/beta, domain swapping, gnat conserved core, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75772.01

構造登録者

Peneff, C.,Mengin-Lecreulx, D.,Bourne, Y. (登録日: 2001-02-01, 公開日: 2001-05-16, 最終更新日: 2023-08-09)

主引用文献

Peneff, C.,Mengin-Lecreulx, D.,Bourne, Y.
The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.
J.Biol.Chem., 276:16328-16334, 2001

PubMed Abstract: The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface but also shed light on the catalytic machinery of GNA1 at an atomic level. Hence, they broaden our understanding of structural features required for GNAT activity, provide structural details for related aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT superfamily members to acquire various specificities.

PubMed: 11278591
DOI: 10.1074/jbc.M009988200

実験手法

X-RAY DIFFRACTION (1.8 Å)