PDBsum entry 1i1d

Transferase

PDB id: 1i1d

Contents

Protein chains

156 a.a. *

Ligands

16G ×3

COA ×2

IMD

Waters ×542

* Residue conservation analysis

PDB id:

1i1d

Name:

Transferase

Title:

Crystal structure of yeast gna1 bound to coa and glnac-6p

Structure:

Glucosamine-phosphate n-acetyltransferase. Chain: a, b, c, d. Synonym: phosphoglucosamine transacetylase. Phosphoglucosamine acetylase. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: yfl017c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.80Å R-factor: 0.183 R-free: 0.223

Authors:

C.Peneff,D.Mengin-Lecreulx,Y.Bourne

Key ref:

C.Peneff et al. (2001). 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. PubMed id: 11278591 DOI: 10.1074/jbc.M009988200

Date:

01-Feb-01 Release date: 16-May-01

Protein chains

P43577  (GNA1_YEAST) -  Glucosamine 6-phosphate N-acetyltransferase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 159 a.a.

Struc: 156 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.3.1.4 - glucosamine-phosphate N-acetyltransferase.
• Pathway: UDP-N-acetylglucosamine Biosynthesis
• Reaction: D-glucosamine 6-phosphate + acetyl-CoA = N-acetyl-D-glucosamine 6-phosphate + CoA + H⁺

D-glucosamine 6-phosphate + acetyl-CoA = N-acetyl-D-glucosamine 6-phosphate (Bound ligand (Het Group name = COA) corresponds exactly) + CoA + H(+) (Bound ligand (Het Group name = 16G) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1074/jbc.M009988200

J Biol Chem 276:16328-16334 (2001)

PubMed id: 11278591

The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.

C.Peneff, D.Mengin-Lecreulx, Y.Bourne.

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.

Selected figure(s)

Figure 3.
Fig. 3. Schematic representation of the proposed GNA1 catalytic mechanism.

Figure 5.
Fig. 5. Structural comparison of substrate binding sites of AANAT , tGCN5, and GNA1. The molecular surfaces around the active site of the AANAT-bisubstrate analog (A), the tGCN5-CoA-H3peptide (B), and the GNA1-CoA-GlcNAc6P complex structures (C) are viewed with a similar orientation. From top to bottom, the serotonin-like moiety and the acetyl group are shown in red, the H3 peptide backbone in yellow, with its reactive Lys-14 side chain in orange, and GlcNAc6P in purple. Structural divergences within the NH[2]- and COOH-terminal regions are highlighted in dark blue and blue, respectively. The 3- 4 insertion loop unique to AANAT is shown in brown.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 16328-16334) copyright 2001.

Figures were selected by an automated process.