Journal article
Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus
CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme.
Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 Å resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems.
Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.
Language: | English |
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Publisher: | International Union of Crystallography |
Year: | 2011 |
Pages: | 201-208 |
ISSN: | 17443091 and 2053230x |
Types: | Journal article |
DOI: | 10.1107/S1744309110052334 |
ORCIDs: | 0000-0003-1689-2712 and Harris, Pernille |
Adenosine Triphosphate Amino Acid Sequence Apoenzymes Binding Sites CTP synthetase Carbon-Nitrogen Ligases Catalysis Conserved Sequence Crystallography, X-Ray Dimerization Escherichia coli Faculty of Science Glutamine Humans Models, Molecular Molecular Sequence Data Molecular Weight Nucleotides Phosphorylation Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Protein Subunits Sequence Homology, Amino Acid Structure-Activity Relationship Substrate Specificity Sulfolobus solfataricus Thermus thermophilus Uridine Triphosphate Water dimer-tetramer equilibrium dimer–tetramer equilibrium nucleotide metabolism