2ukd: Difference between revisions
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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[[Image:2ukd.gif|left|200px]]<br /><applet load="2ukd" size=" | [[Image:2ukd.gif|left|200px]]<br /><applet load="2ukd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ukd, resolution 2.2Å" /> | caption="2ukd, resolution 2.2Å" /> | ||
'''UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP'''<br /> | '''UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP'''<br /> | ||
==Overview== | ==Overview== | ||
UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the | 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 Structure== | ==About this Structure== | ||
2UKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG, ADP and C5P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] Full crystallographic information is available from [http:// | 2UKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=C5P:'>C5P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UKD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:13 2008'' | ||
Revision as of 19:50, 21 February 2008
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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 , and 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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