Structure ofMycobacterium tuberculosisnucleoside diphosphate kinase R80N mutant in complex with citrate
| Autor: | Johann Habersetzer, Alain Dautant, Florian Georgescauld, Lucile Moynié |
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| Přispěvatelé: | Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2013 |
| Předmět: |
Static Electricity
Mutant Biophysics [SDV.BC]Life Sciences [q-bio]/Cellular Biology Random hexamer Crystallography X-Ray Biochemistry Citric Acid Protein Structure Secondary chemistry.chemical_compound Structural Biology Genetics Structural Communications Nucleotide Thermal stability chemistry.chemical_classification Hydrogen bond Chemistry Mycobacterium tuberculosis Salt bridge (protein and supramolecular) Condensed Matter Physics Nucleoside-diphosphate kinase 3. Good health Protein Subunits Crystallography Amino Acid Substitution Nucleoside-Diphosphate Kinase Mutant Proteins Citric acid |
| Zdroj: | Acta Crystallogr F Struct Biol Commun Acta Crystallogr F Struct Biol Commun, 2014, 70 (Pt 1), pp.40-3. ⟨10.1107/S2053230X13034134⟩ |
| ISSN: | 2053-230X |
| Popis: | International audience; The crystal structure of the wild-type nucleoside diphosphate kinase from Mycobacterium tuberculosis at 2.6 Å resolution revealed that the intersubunit salt bridge Arg80-Asp93 contributes to the thermal stability of the hexamer (Tm = 76°C). On mutating Asp93 to Asn to break the salt bridge, the thermal stability dramatically decreased by 27.6°C. Here, on mutating Arg80 to Asn, the thermal stability also significantly decreased by 8.0°C. In the X-ray structure of the R80N mutant solved at 1.9 Å resolution the salt bridge was replaced by intersubunit hydrogen bonds that contribute to the thermal stability of the hexamer. A citrate anion from the crystallization buffer was bound at the bottom of the nucleotide-binding site via electrostatic and hydrogen-bonding interactions with six conserved residues involved in nucleotide binding. Structural analysis shows that the citrate is present at the location of the nucleotide phosphate groups. |
| Databáze: | OpenAIRE |
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