2ukd

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[[Image:2ukd.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2ukd| PDB=2ukd | SCENE= }}
{{STRUCTURE_2ukd| PDB=2ukd | SCENE= }}
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'''UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP'''
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===UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9280438 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9280438}}
==About this Structure==
==About this Structure==
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[[Category: Phosphoryl transfer]]
[[Category: Phosphoryl transfer]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:58:29 2008''

Revision as of 09:58, 29 July 2008

Image:2ukd.png

Template:STRUCTURE 2ukd

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

Template:ABSTRACT PUBMED 9280438

About this Structure

2UKD is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

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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