1nsp
MECHANISM OF PHOSPHATE TRANSFER BY NUCLEOSIDE DIPHOSPHATE KINASE: X-RAY STRUCTURES OF A PHOSPHO-HISTIDINE INTERMEDIATE OF THE ENZYMES FROM DROSOPHILA AND DICTYOSTELIUM
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OverviewOverview
Nucleoside diphosphate kinase (NDP kinase) has a ping-pong mechanism with, a phosphohistidine intermediate. Crystals of the enzymes from, Dictyostelium discoideum and from Drosophila melanogaster were treated, with phosphoramidate, and their X-ray structures were determined at 2.1, and 2.2 A resolution, respectively. The atomic models, refined to R, factors below 20%, show no conformation change relative to the free, proteins. In both enzymes, the active site histidine was phosphorylated on, N delta, and it was the only site of phosphorylation. The phosphate group, interacts with the hydroxyl group of Tyr56 and with protein-bound water, molecules. Its environment is compared with that of phosphohistidines in, succinyl-CoA synthetase and in phosphocarrier proteins. The X-ray, structures of phosphorylated NDP kinase and of previously determined, complexes with nucleoside diphosphates provide a basis for modeling the, Michaelis complex with a nucleoside triphosphate, that of the, phosphorylated protein with a nucleoside diphosphate, and the transition, state of the phosphate transfer reaction in which the gamma-phosphate is, pentacoordinated.
About this StructureAbout this Structure
1NSP is a Single protein structure of sequence from Dictyostelium discoideum. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium., Morera S, Chiadmi M, LeBras G, Lascu I, Janin J, Biochemistry. 1995 Sep 5;34(35):11062-70. PMID:7669763
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