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PDBsum entry 1vkl
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Phosphotransferase
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PDB id
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1vkl
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Contents |
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* Residue conservation analysis
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Biochemistry
32:48-57
(1993)
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PubMed id:
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Structural changes at the metal ion binding site during the phosphoglucomutase reaction.
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W.J.Ray,
C.B.Post,
Y.Liu,
G.I.Rhyu.
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ABSTRACT
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An electron density map of the reactive, Cd2+ form of crystalline
phosphoglucomutase from X-ray diffraction studies shows that the enzymic
phosphate donates a nonbridging oxygen to the ligand sphere of the bound metal
ion, which appears to be tetracoordinate. 31P and 113Cd NMR spectroscopy are
used to assess changes in the properties of bound Cd2+ produced by
substrate/product and by substrate/product analog inhibitors. The approximately
50 ppm downfield shift of the 113Cd resonance on formation of the complex of
dephosphoenzyme and glucose 1,6-bisphosphate is associated with the initial
sugar-phosphate binding step and likely involves a change in the geometry of the
coordinating ligands. This interpretation is supported by spectral studies
involving various complexes of the active Co2+ and Ni(2+)-enzyme. In addition,
there is a loss of the 31P-113Cd J coupling that characterizes the monophosphate
complexes of the Cd2+ enzyme either during or immediately after the PO3-
transfer step that produces the bisphosphate complex, indicating a further
change at the metal binding site. The implications of these observations with
respect to the PO3- transfer process in the phosphoglucomutase reaction are
considered. The apparent plasticity of the ligand sphere of the active site
metal ion in this system may allow a single metal ion to act as a chaperone for
a nonbridging oxygen during PO3- transfer or to allow a change in metal ion
coordination during catalysis. A general NMR line shape/chemical-exchange
analysis for evaluating binding in protein-ligand systems when exchange is
intermediate to fast on the NMR time scale is described. Its application to the
present system involves multiple exchange sites that depend on a single binding
rate, thereby adding further constraints to the analysis.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Kitchen,
R.E.Saunders,
and
J.Warwicker
(2008).
Charge environments around phosphorylation sites in proteins.
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BMC Struct Biol,
8,
19.
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C.A.Regni,
P.A.Tipton,
and
L.J.Beamer
(2000).
Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa.
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Acta Crystallogr D Biol Crystallogr,
56,
761-762.
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G.Minasov,
M.Teplova,
G.C.Stewart,
E.V.Koonin,
W.F.Anderson,
and
M.Egli
(2000).
Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP.
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Proc Natl Acad Sci U S A,
97,
6328-6333.
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PDB codes:
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R.S.Ehrlich,
and
R.F.Colman
(1995).
Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart.
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Biochim Biophys Acta,
1246,
135-141.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
