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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.
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PubMed id
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Abstract
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UMP/CMP-kinase (UK) from the slime mold Dictyostelium discoideum has been
purified to high homogeneity and co-crystallized with the bisubstrate inhibitor
P1-(adenosine 5')-P5-(uridine 5')-pentaphosphate (UP5A). UP5A binds to UK with a
dissociation constant (Kd) of 3 +/- 0.5 nM at 25 degrees C and pH 7.5. This is
some 50-fold tighter than the binding of P1,P5-(diadenosine 5')-pentaphosphate
(AP5A, Kd = 160 +/- 15 nM). AP5A is a bisubstrate inhibitor that is specific for
adenylate kinase. The crystals have the symmetry of the tetragonal space group
P4(1)2(1)2 or its enantiomorph P4(3)2(1)2. The unit cell dimensions are a = b =
78.5 A and c = 101.4 A. The crystals diffract to a Bragg spacing of 2.1 A.
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