Motion in UMP/CMP kinase [ucmpkin]

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Classification [D-h-2]

Structures
1TEV Apo structure (human)
3UKD Bound to UMP/ADP/AlF3 (Dictyostelium) [ PartsList ]

Description
Domain closure upon substrate binding.

References
L Wiesmuller, A A Noegel, O Barzu, G Gerisch, M Schleicher (1990). cDNA-derived sequence of UMP-CMP kinase from Dictyostelium discoideum and expression of the enzyme in Escherichia coli. J Biol Chem, 265:6339-45 [Medline info for 2156849]
Dario Segura-Pena, Nikolina Sekulic, Stephan Ort, Manfred Konrad, Arnon Lavie (2004). Substrate-induced conformational changes in human UMP/CMP kinase. J Biol Chem, 279:33882-9 [Medline info for 15163660]
L Wiesmuller, K Scheffzek, W Kliche, R S Goody, A Wittinghofer, J Reinstein (1995). Crystallization and preliminary X-ray analysis of UMP/CMP-kinase from Dictyostelium discoideum with the specific bisubstrate inhibitor P1-(adenosine 5')-P5-(uridine 5')-pentaphosphate (UP5A). FEBS Lett, 363:22-4 [Medline info for 7729545]
K Scheffzek, W Kliche, L Wiesmuller, J Reinstein (1996). Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 A: implications for water-mediated specificity. Biochemistry, 35:9716-27 [Medline info for 8703943]
I Schlichting, J Reinstein (1997). Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry, 36:9290-6 [Medline info for 9280438]

GO terms associated with structures
Molecular functionphosphotransferase activity, phosphate group as acceptor, nucleotide kinase activity, ATP binding
Biological processnucleobase, nucleoside, nucleotide and nucleic acid metabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu