1NSP

MECHANISM OF PHOSPHATE TRANSFER BY NUCLEOSIDE DIPHOSPHATE KINASE: X-RAY STRUCTURES OF A PHOSPHO-HISTIDINE INTERMEDIATE OF THE ENZYMES FROM DROSOPHILA AND DICTYOSTELIUM

Summary for 1NSP

• Entry DOI: 10.2210/pdb1nsp/pdb
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE (2 entities in total)
• Functional Keywords: nucleoside triphosphate: nucleoside diphosphate, phosphotransferase
• Biological source: Dictyostelium discoideum
• Cellular location: Cytoplasm: P22887
• Total number of polymer chains: 1
• Total formula weight: 16896.32

Authors

Janin, J.,Morera, S.,Chiadmi, M.,Lebras, G.,Lascu, I. (deposition date: 1995-04-18, release date: 1995-07-10, Last modification date: 2024-06-05)

Primary citation

Morera, S.,Chiadmi, M.,LeBras, G.,Lascu, I.,Janin, J.
Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium.
Biochemistry, 34:11062-11070, 1995

PubMed Abstract: 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.

PubMed: 7669763
DOI: 10.1021/bi00035a011

Experimental method

X-RAY DIFFRACTION (2.1 Å)