1N8T

The crystal structure of phosphoglucose isomerase from rabbit muscle

Summary for 1N8T

• Entry DOI: 10.2210/pdb1n8t/pdb
• Descriptor: Glucose-6-phosphate isomerase (2 entities in total)
• Functional Keywords: aldose-ketose isomerase, cytokine, glycolysis, isomerase
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm: Q9N1E2
• Total number of polymer chains: 2
• Total formula weight: 125392.71

Authors

Davies, C.,Muirhead, H. (deposition date: 2002-11-21, release date: 2003-03-04, Last modification date: 2024-02-14)

Primary citation

Davies, C.,Muirhead, H.
Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function.
Acta Crystallogr.,Sect.D, 59:453-465, 2003

PubMed Abstract: Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis.

PubMed: 12595702
DOI: 10.1107/S0907444902023387

Experimental method

X-RAY DIFFRACTION (2.5 Å)