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PDBsum entry 2f90
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References listed in PDB file
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Key reference
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Title
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Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
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Authors
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Y.Wang,
L.Liu,
Z.Wei,
Z.Cheng,
Y.Lin,
W.Gong.
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Ref.
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J Biol Chem, 2006,
281,
39642-39648.
[DOI no: ]
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PubMed id
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Abstract
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Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series
of intermolecular phosphoryl group transfer reactions. Its main function is to
synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. In
this paper, we directly observed real-time motion of the enzyme active site and
the substrate during phosphoryl transfer. A series of high resolution crystal
structures of human bisphosphoglycerate mutase co-crystallized with
2,3-bisphosphoglycerate, representing different time points in the phosphoryl
transfer reaction, were solved. These structures not only clarify the argument
concerning the substrate binding mode for this enzyme family but also depict the
entire process of the key histidine phosphorylation as a "slow movie".
It was observed that the enzyme conformation continuously changed during the
different states of the reaction. These results provide direct evidence for an
"in line" phosphoryl transfer mechanism, and the roles of some key
residues in the phosphoryl transfer process are identified.
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Figure 1.
FIGURE 1. A F[o] - F[c] electron density map (contoured at
3.5  , purple cage) at the
active site when the side chain of His-11 and the ligand are
omitted. A (structure 1), co-crystallized with 2,3-BPG at 4
°C. B (structure 2), co-crystallized with 2,3-BPG at 16
°C for less than 16 days. C (structure 3), only 3-PGA
binding. D (structure 4), co-crystallized with 2,3-BPG at 16
°C for 17 days. Extra F[o] - F[c] electron density
(contoured at 3 , blue cage) exists
when two water molecules and 3-PGA are modeled in. E (structure
5), co-crystallized with  and
3-PGA.
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Figure 4.
FIGURE 4. Schematic of the interactions between the ligand
and human BPGM with all interactions between the ligand and
residues depicted as dashed lines and labeled with the bond
lengths (Å). A, interactions between 2,3-BPG and BPGM in
the reacting state. B, interaction between 3-PGA and the
phosphorylated enzyme.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
39642-39648)
copyright 2006.
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