Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
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Summary
A binary complex of malate dehydrogenase from the thermophilic bacterium Thermus flavus (tMDH) with NADH has been crystallized from poly(ethylene glycol) 3500, pH 8.5, yielding diffraction-quality crystals in space group P2(1)2-2-1-2(2)2, with comparison with cMDH revealing that both tMDH subunits more closely resemble the B subunit of c MDH
- Type
- article
- Published
- 1993-04-20
- Cited by
- 139
- References
- 27
- OpenAlex
- https://openalex.org/W2054576968
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34406953
Keywords
Thermostability, Thermus, Thermophile, Citation, Computer science
References
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Cited by
- Intrasteric inhibition in redox signalling: light activation of NADP-malate dehydrogenase
- (Beta alpha)8‐barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima.
- Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water.
- Using Protein Design to Understand the Role of Electrostatic Interactions on Calcium Binding Affinity and Molecular Recognition
- Tetrameric and dimeric malate dehydrogenase isoenzymes in Trypanosoma cruzi epimastigotes.
- Isocitrate dehydrogenase, malate dehydrogenase, and glutamate dehydrogenase from Archaeoglobus fulgidus.
- Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
- Structural studies of lumazine synthases : Thermostability, catalytic mechanism and molecular assembly
- Structure and expression of a pyrimidine gene cluster from the extreme thermophile Thermus strain ZO5
- Overexpression and purification of membrane proteins in yeast
- Rigidity versus flexibility: the dilemma of understanding protein thermal stability
- Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant.
- Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction.
- Light‐activation of NADP‐malate dehydrogenase: A highly controlled process for an optimized function
- Directed Mutagenesis of the Conserved Asparagine Residues of Bacillus Stearothermophilus Leucine Aminopeptidase II
- X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons.
- Probing the instabilities in the dynamics of helical fragments from mouse PrPC.
- Crystal structure of recombinant triosephosphate isomerase from bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three‐dimensional structures points to the importance of hydrophobic interactions
- Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase.
- Macromolecular crowding and the steady-state kinetics of malate dehydrogenase.
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