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PDBsum entry 4my4
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References listed in PDB file
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Key reference
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Title
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Complete catalytic cycle of cofactor-Independent phosphoglycerate mutase involves a spring-Loaded mechanism.
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Authors
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A.Roychowdhury,
A.Kundu,
M.Bose,
A.Gujar,
S.Mukherjee,
A.K.Das.
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Ref.
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Febs J, 2015,
282,
1097-1110.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Cofactor-independent phosphoglycerate mutase (iPGM), an important enzyme in
glycolysis and gluconeogenesis, catalyses the isomerization of 2- and
3-phosphoglycerates by an Mn(2+) -dependent phospho-transfer mechanism via a
phospho-enzyme intermediate. Crystal structures of bi-domain iPGM from
Staphylococcus aureus, together with substrate-bound forms, have revealed a new
conformation of the enzyme, representing an intermediate state of domain
movement. The substrate-binding site and the catalytic site are present in two
distinct domains in the intermediate form. X-ray crystallography complemented by
simulated dynamics has enabled delineation of the complete catalytic cycle,
which includes binding of the substrate, followed by its positioning into the
catalytic site, phospho-transfer and finally product release. The present work
describes a novel mechanism of domain movement controlled by a hydrophobic patch
that is exposed on domain closure and acts like a spring to keep the protein in
open conformation. Domain closing occurs after substrate binding, and is
essential for phospho-transfer, whereas the open conformation is a prerequisite
for efficient substrate binding and product dissociation. A new model of
catalysis has been proposed by correlating the hinge-bending motion with the
phospho-transfer mechanism.
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