1N8T

Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function.

(2003) Acta Crystallogr D Biol Crystallogr 59: 453-465

• PubMed: 12595702 Search on PubMed
• DOI: https://doi.org/10.1107/s0907444902023387
• Primary Citation of Related Structures:  
  1N8T


• 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.

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Organizational Affiliation: 

Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA. [email protected]