1DQR

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR

Summary for 1DQR

• Entry DOI: 10.2210/pdb1dqr/pdb
• Descriptor: PHOSPHOGLUCOSE ISOMERASE, 6-PHOSPHOGLUCONIC ACID (3 entities in total)
• Functional Keywords: alpha-beta sandwich domains, anti-parallel beta sheet, parallel beta sheet, isomerase
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 2
• Total formula weight: 125945.11

Authors

Bahnson, B.J.,Jeffery, C.J.,Ringe, D.,Petsko, G.A. (deposition date: 2000-01-05, release date: 2000-02-09, Last modification date: 2024-02-07)

Primary citation

Jeffery, C.J.,Bahnson, B.J.,Chien, W.,Ringe, D.,Petsko, G.A.
Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator.
Biochemistry, 39:955-964, 2000

PubMed Abstract: The multifunctional protein phosphoglucose isomerase, also known as neuroleukin, autocrine motility factor, and differentiation and maturation mediator, has different roles inside and outside the cell. In the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine. We have determined the three-dimensional structure of rabbit muscle phosphoglucose isomerase complexed with the competitive inhibitor D-gluconate 6-phosphate by X-ray crystallography at 2.5 A resolution. The structure shows that the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit. The location of the bound D-gluconate 6-phosphate inhibitor leads to the identification of residues involved in substrate specificity (Ser209, Ser159, Thr214, Thr217, and Thr211). The results of previously published kinetic studies suggest that a lysine and a histidine are involved in the catalytic mechanism. The crystal structure suggests active site residues Lys518 and His388 might be these residues. In addition, the positions of amino acid residues that are substituted in the genetic disease nonspherocytic hemolytic anemia suggest how these substitutions can result in altered catalysis or protein stability.

PubMed: 10653639
DOI: 10.1021/bi991604m

Experimental method

X-RAY DIFFRACTION (2.5 Å)