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PDBsum entry 4ukd
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References listed in PDB file
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Key reference
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Title
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Structures of active conformations of ump kinase from dictyostelium discoideum suggest phosphoryl transfer is associative.
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Authors
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I.Schlichting,
J.Reinstein.
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Ref.
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Biochemistry, 1997,
36,
9290-9296.
[DOI no: ]
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PubMed id
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Abstract
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UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the specific
transfer of the terminal phosphate of ATP to UMP or CMP. Crystal structures of
UmpKdicty with substrates and the transition state analogs AlF3 or BeF2 that
lock UmpKdicty in active conformations were solved. The positions of the
catalytic Mg2+ and the highly conserved lysine of the P loop are virtually
invariant in the different structures. In contrast, catalytic arginines move to
stabilize charges that develop during this reaction. The location of the
arginines indicates formation of negative charges during the reaction at the
transferred phosphoryl group, but not at the phosphate bridging oxygen atoms.
This is consistent with an associative phosphoryl transfer mechanism but not
with a dissociative one.
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Secondary reference #1
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Title
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Crystal structure of the complex of ump/cmp kinase from dictyostelium discoideum and the bisubstrate inhibitor p1-(5'-Adenosyl) p5-(5'-Uridyl) pentaphosphate (up5a) and mg2+ at 2.2 a: implications for water-Mediated specificity.
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Authors
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K.Scheffzek,
W.Kliche,
L.Wiesmüller,
J.Reinstein.
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Ref.
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Biochemistry, 1996,
35,
9716-9727.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Crystallization and preliminary X-Ray analysis of ump/cmp-Kinase from dictyostelium discoideum with the specific bisubstrate inhibitor p1-(Adenosine 5')-P5-(Uridine 5')-Pentaphosphate (up5a).
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Authors
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L.Wiesmüller,
K.Scheffzek,
W.Kliche,
R.S.Goody,
A.Wittinghofer,
J.Reinstein.
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Ref.
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FEBS Lett, 1995,
363,
22-24.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Cdna-Derived sequence of ump-Cmp kinase from dictyostelium discoideum and expression of the enzyme in escherichia coli.
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Authors
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L.Wiesmüller,
A.A.Noegel,
O.Bârzu,
G.Gerisch,
M.Schleicher.
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Ref.
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J Biol Chem, 1990,
265,
6339-6345.
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PubMed id
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