Molecular modeling and dynamics studies of cytidylate kinase from Mycobacterium tuberculosis H37Rv
| Autor: | Walter Filgueira de Azevedo, Luiz Augusto Basso, Cristopher Z. Schneider, Ana Luiza Vivan, Rafael Andrade Caceres, Diógenes Santiago Santos, Luis Fernando Saraiva Macedo Timmers |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Cytidine monophosphate Molecular model Stereochemistry Molecular Sequence Data Biology Ligands Catalysis Inorganic Chemistry chemistry.chemical_compound Cytidine Monophosphate Escherichia coli Computer Simulation Amino Acid Sequence Physical and Theoretical Chemistry UMP kinase chemistry.chemical_classification Nucleoside-phosphate kinase Organic Chemistry Cytidine Mycobacterium tuberculosis Protein Structure Tertiary Computer Science Applications carbohydrates (lipids) Enzyme Computational Theory and Mathematics chemistry Biochemistry Nucleoside-Phosphate Kinase Sequence Alignment Nucleoside Cytidylate kinase |
| Zdroj: | Journal of Molecular Modeling. 14:427-434 |
| ISSN: | 0948-5023 1610-2940 |
| DOI: | 10.1007/s00894-008-0291-2 |
| Popis: | Bacterial cytidylate kinase or cytidine monophosphate kinase (CMP kinase) catalyses the phosphoryl transfer from ATP to CMP and dCMP, resulting in the formation nucleoside diphosphates. In eukaryotes, CMP/UMP kinase catalyses the conversion of UMP and CMP to, respectively, UDP and CDP with high efficiency. This work describes for the first time a model of bacterial cytidylate kinase or cytidine monophosphate kinase (CMP kinase) from mycobacterium tuberculosis (MtCMPK). We modeled MtPCMPK in apo form and in complex with cytidine 5'-monophosphate (CMP) to try to determine the structural basis for specificity. Comparative analysis of the model of MtCMPK allowed identification of structural features responsible for ligand affinities. Analysis of the molecular dynamics simulations of these two systems indicates the structural features responsible for the stability of the structure, and may help in the identification of new inhibitors for this enzyme. |
| Databáze: | OpenAIRE |
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