PDBsum entry 2vez

Transferase

PDB id

2vez

Loading ...

Contents

			Protein chain

					165 a.a. *

			Ligands

					ACO


					G6P


					PO4

			Waters ×204

* Residue conservation analysis

PDB id:

2vez

Links

Name:

Transferase

Title:

Afgna1 crystal structure complexed with acetyl-coa and glucose-6p gives new insights into catalysis

Structure:

Putative glucosamine 6-phosphate acetyltransferase. Chain: a. Synonym: glucosamine-6-phosphate n-acetyltransferase. Engineered: yes

Source:

Aspergillus fumigatus. Sartorya fumigata. Organism_taxid: 5085. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.45Å

R-factor:

0.169

R-free:

0.219

Authors:

R.Hurtado-Guerrero,O.Raimi,S.Shepherd,D.M.F.Van Aalten

Key ref:

R.Hurtado-Guerrero et al. (2007). Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex. Febs Lett, 581, 5597-5600. PubMed id: 18005663

Date:

27-Oct-07

Release date:

10-Mar-09

PROCHECK

	Headers

	References

Protein chain

Q4WCU5 (Q4WCU5_ASPFU) - Glucosamine 6-phosphate acetyltransferase, putative from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

Seq: Struc:					190 a.a. 165 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.3.1.4 - glucosamine-phosphate N-acetyltransferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

UDP-N-acetylglucosamine Biosynthesis

Reaction:

D-glucosamine 6-phosphate + acetyl-CoA = N-acetyl-D-glucosamine 6-phosphate + CoA + H⁺

D-glucosamine 6-phosphate
Bound ligand (Het Group name = ACO)
corresponds exactly

acetyl-CoA
Bound ligand (Het Group name = G6P)
matches with 88.24% similarity

N-acetyl-D-glucosamine 6-phosphate

CoA

H(+)

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

reference

	Febs Lett 581:5597-5600 (2007)
PubMed id: 18005663

Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex.
R.Hurtado-Guerrero, O.Raimi, S.Shepherd, D.M.van Aalten.

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22868768

H.C.Dorfmueller, W.Fang, F.V.Rao, D.E.Blair, H.Attrill, and D.M.van Aalten (2012).
Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1.

Acta Crystallogr D Biol Crystallogr, 68, 1019-1029.

PDB codes:

4ag7 4ag9

18778413

J.B.Vicente, G.M.Ehrenkaufer, L.M.Saraiva, M.Teixeira, and U.Singh (2009).
Entamoeba histolytica modulates a complex repertoire of novel genes in response to oxidative and nitrosative stresses: implications for amebic pathogenesis.

Cell Microbiol, 11, 51-69.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.