3CXP

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

Summary for 3CXP

• Entry DOI: 10.2210/pdb3cxp/pdb
• Related: 3CXQ 3CXS
• Descriptor: Glucosamine 6-phosphate N-acetyltransferase, CHLORIDE ION (3 entities in total)
• Functional Keywords: gna1, acyltransferase, endosome, golgi apparatus, membrane, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane; Peripheral membrane protein: Q96EK6
• Total number of polymer chains: 1
• Total formula weight: 20753.53

Authors

Wang, J.,Liu, X.,Li, L.-F.,Su, X.-D. (deposition date: 2008-04-25, release date: 2008-09-16, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.01 Å)