2UKD

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

Summary for 2UKD

• Entry DOI: 10.2210/pdb2ukd/pdb
• Descriptor: URIDYLMONOPHOSPHATE/CYTIDYLMONOPHOSPHATE KINASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: nucleoside monophosphate kinase, nmp kinase, phosphoryl transfer, transferase
• Biological source: Dictyostelium discoideum
• Total number of polymer chains: 1
• Total formula weight: 22745.56

Authors

Schlichting, I.,Reinstein, J. (deposition date: 1997-05-20, release date: 1998-05-20, Last modification date: 2024-02-21)

Primary citation

Schlichting, I.,Reinstein, J.
Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative.
Biochemistry, 36:9290-9296, 1997

PubMed Abstract: 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.

PubMed: 9280438
DOI: 10.1021/bi970974c

Experimental method

X-RAY DIFFRACTION (2.2 Å)