1I12

CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA

Summary for 1I12

• Entry DOI: 10.2210/pdb1i12/pdb
• Related: 1I1D 1I21
• Descriptor: GLUCOSAMINE-PHOSPHATE N-ACETYLTRANSFERASE, ACETYL COENZYME *A, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: gnat, alpha/beta, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 4
• Total formula weight: 76412.54

Authors

Peneff, C.,Mengin-Lecreulx, D.,Bourne, Y. (deposition date: 2001-01-30, release date: 2001-05-16, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)