PDBsum entry 2wu8

Isomerase

PDB id: 2wu8

Contents

Protein chain

549 a.a. *

Ligands

SO4 ×2

Waters ×282

* Residue conservation analysis

PDB id:

2wu8

Name:

Isomerase

Title:

Structural studies of phosphoglucose isomerase from mycobacterium tuberculosis h37rv

Structure:

Glucose-6-phosphate isomerase. Chain: a. Fragment: residues 7-553. Synonym: phosphoglucose isomerase, phosphohexose isomerase, gpi, pgi, phi. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.25Å R-factor: 0.183 R-free: 0.223

Authors:

K.Anand

Key ref:

K.Anand et al. (2010). Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 490-497. PubMed id: 20445242

Date:

01-Oct-09 Release date: 27-Oct-09

Protein chain

P9WN69  (G6PI_MYCTU) -  Glucose-6-phosphate isomerase from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 553 a.a.

Struc: 549 a.a.*

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

Enzyme reactions

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

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

Added reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 66:490-497 (2010)

PubMed id: 20445242

Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.

K.Anand, D.Mathur, A.Anant, L.C.Garg.

ABSTRACT

Phosphoglucose isomerase (PGI) plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. PGI is also known to act as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator. Here, the first crystal structure of PGI from Mycobacterium tuberculosis H37Rv (Mtb) is reported. The structure was refined at 2.25 A resolution and revealed the presence of one molecule in the asymmetric unit with two globular domains. As known previously, the active site of Mtb PGI contains conserved residues including Glu356, Glu216 and His387 (where His387 is from the neighbouring molecule). The crystal structure of Mtb PGI was observed to be rather more similar to human PGI than other nonbacterial PGIs, with only a few differences being detected in the loops, arm and hook regions of the human and Mtb PGIs, suggesting that the M. tuberculosis enzyme uses the same enzyme mechanism.