Crystallization behaviour of glyceraldehyde dehydrogenase fromThermoplasma acidophilum
| Autor: | Fabian Steffler, Ivana Kuta Smatanova, Volker Sieber, Iuliia Iermak, Oksana Degtjarik |
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| Rok vydání: | 2015 |
| Předmět: |
Thermoplasma
Molecular Sequence Data Biophysics Dehydrogenase Biochemistry Research Communications chemistry.chemical_compound X-Ray Diffraction Structural Biology Glyceraldehyde Genetics Amino Acid Sequence Saturated mutagenesis biology Artificial enzyme Thermoplasma acidophilum Space group Condensed Matter Physics biology.organism_classification Crystallography chemistry biology.protein Crystallization Sugar Alcohol Dehydrogenases Monoclinic crystal system |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 71:1475-1480 |
| ISSN: | 2053-230X |
| Popis: | The glyceraldehyde dehydrogenase fromThermoplasma acidophilum(TaAlDH) is a microbial enzyme that catalyzes the oxidation of D-glyceraldehyde to D-glycerate in the artificial enzyme cascade designed for the conversion of glucose to the organic solvents isobutanol and ethanol. Various mutants ofTaAlDH were constructed by a random approach followed by site-directed and saturation mutagenesis in order to improve the properties of the enzyme that are essential for its functioning within the cascade. Two enzyme variants, wild-typeTaAlDH (TaAlDHwt) and an F34M+S405N variant (TaAlDH F34M+S405N), were successfully crystallized. Crystals ofTaAlDHwt belonged to the monoclinic space groupP1211 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 Å.TaAlDH F34M+S405N crystallized in two different space groups: triclinicP1 with 16 molecules per asymmetric unit and monoclinicC121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 Å for theP1 andC121 crystals, respectively. |
| Databáze: | OpenAIRE |
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