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PDBsum entry 1jlh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps.
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Authors
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A.T.Cordeiro,
P.H.Godoi,
C.H.Silva,
R.C.Garratt,
G.Oliva,
O.H.Thiemann.
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Ref.
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Biochim Biophys Acta, 2003,
1645,
117-122.
[DOI no: ]
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PubMed id
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Abstract
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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.
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