4ukd

UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, UDP, BERYLLIUM FLUORIDE

spinqualitylabelsall models 4ukd, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ukd is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ADP, BF2, MG, UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCY_DICDI This UMP-CMP kinase uses preferentially ATP as phosphate donor and is specific for UMP and CMP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UMP/CMP kinase

Proteopedia Page Contributors and Editors (what is this?)

OCA