PDBsum entry: 1q50

Isomerase

PDB id: 1q50

Contents

Protein chain

561 a.a. *

Waters ×216

* Residue conservation analysis

PDB id:

1q50

Name:

Isomerase

Title:

Phosphoglucose isomerase from leishmania mexicana.

Structure:

Glucose-6-phosphate isomerase. Chain: a. Synonym: gpi, phosphoglucose isomerase, pgi, phosphohexose phi. Engineered: yes

Source:

Leishmania mexicana. Organism_taxid: 5665. Gene: pgi. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

2.60Å R-factor: 0.198 R-free: 0.250

Authors:

A.T.Cordeiro,P.A.M.Michels,L.F.Delboni,O.H.Thiemann

Key ref:

A.T.Cordeiro et al. (2004). The crystal structure of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features. Eur J Biochem, 271, 2765-2772. PubMed id: 15206941 DOI: 10.1111/j.1432-1033.2004.04205.x

Date:

05-Aug-03 Release date: 29-Jun-04

Protein chain

P42861  (G6PI_LEIME) -  Glucose-6-phosphate isomerase

Seq: 605 a.a.

Struc: 561 a.a.

Enzyme reactions

• Enzyme class: E.C.5.3.1.9 - Glucose-6-phosphate isomerase.
• Reaction: D-glucose 6-phosphate = D-fructose 6-phosphate

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

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: gluconeogenesis (2 terms)
• Biochemical function: isomerase activity (2 terms)

Added reference

DOI no: 10.1111/j.1432-1033.2004.04205.x

Eur J Biochem 271:2765-2772 (2004)

PubMed id: 15206941

The crystal structure of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features.

A.T.Cordeiro, P.A.Michels, L.F.Delboni, O.H.Thiemann.

ABSTRACT

Glucose-6-phosphate isomerase catalyzes the reversible aldose-ketose isomerization of D-glucose-6-phosphate to D-fructose-6-phosphate in glycolysis and gluconeogenesis, and in the recycling of hexose-6-phosphate in the pentose phosphate pathway. The unicellular protozoans, Trypanosoma brucei, T. cruzi and Leishmania spp., of the order Kinetoplastida are important human parasites responsible for African sleeping sickness, Chagas' disease and leishmaniases, respectively. In these parasites, glycolysis is an important (and in some cases the only) metabolic pathway for ATP supply. The first seven of the 10 enzymes that participate in glycolysis, as well as an important fraction of the enzymes of the pentose phosphate pathway, are compartmentalized in peroxisome-like organelles called glycosomes. The dependence of the parasites on glycolysis, the importance of the pentose phosphate pathway in defense against oxidative stress, and the unique compartmentalization of these pathways, point to the enzymes contained in the glycosome as potential targets for drug design. The present report describes the first crystallographic structure of a parasite (Leishmania mexicana) glucose-6-phosphate isomerase. A comparison of the atomic structure of L. mexicana, human and other mammalian PGIs, which highlights unique features of the parasite's enzyme, is presented.

Selected figure(s)

Figure 1.
Fig. 1. Cartoon representation of Leishmania mexicana glucose-6-phosphate isomerase(PGI-Lm). The native enzyme is a homodimer with the monomer subunit formed by two / sandwich domains (large and small domains) and a C-terminal -helix segment that embraces the adjacent monomer. The catalytic residues are distributed among the small domain and C-terminal segment from one monomer, and at the large domain from the other monomer.

Figure 4.
Fig. 4. Stereoview of the active site of N-terminally deleted glucose-6-phosphate isomerase from Leishmania mexicana(dPGI-Lm) with bound D-fructose-6-phosphate(D-Fru6P).(A) Electron density map 2 [A]|F[o]|-D|F[c]| (contoured at 1 ), colored green, yellow and magenta for loop A, loop B and D-Fru6P, respectively; monomers A and B are represented by gray and blue sticks, respectively. (B) Hydrogen bonds between D-Fru6P and dPGI-Lm residues are colored yellow, while red dot lines represent the separation between atoms that form hydrogen bonds in the D-Fru6P/rabbit PGI complex [21]. These distances indicate that loops A and B from PGI-Lm should move 5 Å to place D-Fru6P in a similar orientation described for D-Fru6P/rabbit PGI.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2004, 271, 2765-2772) copyright 2004.

Figures were selected by an automated process.