1JLH

Human Glucose-6-phosphate Isomerase

Summary for 1JLH

• Entry DOI: 10.2210/pdb1jlh/pdb
• Related: 1dqr 1g98 1hox 1iat
• Descriptor: phosphoglucose isomerase (2 entities in total)
• Functional Keywords: glycolysis, glyconeogenesis, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P06744
• Total number of polymer chains: 4
• Total formula weight: 252919.52

Authors

Cordeiro, A.T. (deposition date: 2001-07-16, release date: 2003-02-11, Last modification date: 2023-08-16)

Primary citation

Cordeiro, A.T.,Godoi, P.H.C.,Silva, C.H.T.P.,Garratt, R.C.,Oliva, G.,Thiemann, O.H.
Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps
BIOCHIM.BIOPHYS.ACTA, 1645:117-122, 2003

PubMed 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 A. 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.

PubMed: 12573240
DOI: 10.1016/S1570-9639(02)00464-8

Experimental method

X-RAY DIFFRACTION (2.1 Å)