2ukd

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Revision as of 15:00, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2ukd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ukd, resolution 2.2Å" /> '''UMP/CMP KINASE FROM S...)
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File:2ukd.gif


2ukd, resolution 2.2Å

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UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP

OverviewOverview

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.

About this StructureAbout this Structure

2UKD is a Single protein structure of sequence from Dictyostelium discoideum with MG, ADP and C5P as ligands. Active as Cytidylate kinase, with EC number 2.7.4.14 Full crystallographic information is available from OCA.

ReferenceReference

Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative., Schlichting I, Reinstein J, Biochemistry. 1997 Aug 5;36(31):9290-6. PMID:9280438

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