Affordable Access

Publisher Website

Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
1570-9639
Publisher
Elsevier
Publication Date
Volume
1645
Issue
2
Identifiers
DOI: 10.1016/s1570-9639(02)00464-8
Keywords
  • Human Phosphoglucose Isomerase
  • Glycolysis
  • Isomerization Mechanism
Disciplines
  • Biology

Abstract

Abstract The second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose–ketose isomerization. Here we describe the human recombinant PGI structure (hPGI) solved in the absence of active site ligands. Crystals isomorphous to those previously reported were used to collect a 94% complete data set to a limiting resolution of 2.1 Å. From the comparison between the free active site hPGI structure and the available human and rabbit PGI (rPGI) structures, a mechanism for protein initial catalytic steps is proposed. Binding of the phosphate moiety of the substrate to two distinct elements of the active site is responsible for driving a series of structural changes resulting in the polarisation of the active site histidine, priming it for the initial ring-opening step of catalysis.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Crystal structure of human phosphoglucose isomeras...

on Biochimica et Biophysica Acta Feb 21, 2003

The crystal structure of human phosphoglucose isom...

on Journal of Molecular Biology Jun 01, 2001

The crystal structure of human phosphoglucose isom...

on Journal of Molecular Biology Jun 01, 2001

Human phosphoglucose isomerase: expression, purifi...

on Acta Crystallographica Section... April 2001
More articles like this..