X-ray structure of nucleoside diphosphate kinase
Autor: | Joël Janin, M. Véron, Christian Dumas, R. Fourme, Ioan Lascu, V. Wallet, Philippe Glaser, M.-L. Lacombe, Solange Moréra |
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Rok vydání: | 1992 |
Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Adenylate kinase MAP3K7 General Biochemistry Genetics and Molecular Biology MAP2K7 TANK-binding kinase 1 Sequence Homology Nucleic Acid Animals Dictyostelium Amino Acid Sequence Molecular Biology Monomeric GTP-Binding Proteins Crystallography General Immunology and Microbiology biology Base Sequence General Neuroscience Cyclin-dependent kinase 2 Cyclin-dependent kinase 3 Proteins NM23 Nucleoside Diphosphate Kinases Biochemistry Mutagenesis Nucleoside-Diphosphate Kinase biology.protein Cyclin-dependent kinase 7 Casein kinase 2 Transcription Factors Research Article |
Zdroj: | The EMBO journal. 11(9) |
ISSN: | 0261-4189 |
Popis: | The X-ray structure of a point mutant of nucleoside diphosphate kinase (NDP kinase) from Dictyostelium discoideum has been determined to 2.2 A resolution. The enzyme is a hexamer made of identical subunits with a novel mononucleotide binding fold. Each subunit contains an alpha/beta domain with a four stranded, antiparallel beta-sheet. The topology is different from adenylate kinase, but identical to the allosteric domain of Escherichia coli ATCase regulatory subunits, which bind mononucleotides at an equivalent position. Dimer contacts between NDP kinase subunits within the hexamer are similar to those in ATCase. Trimer contacts involve a large loop of polypeptide chain that bears the site of the Pro----Ser substitution in Killer of prune (K-pn) mutants of the highly homologous Drosophila enzyme. Properties of Drosophila NDP kinase, the product of the awd developmental gene, and of the human enzyme, the product of the nm23 genes in tumorigenesis, are discussed in view of the three-dimensional structure and of possible interactions of NDP kinase with other nucleotide binding proteins. |
Databáze: | OpenAIRE |
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