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Literature summary for 2.7.4.3 extracted from

  • Moon, S.; Bae, E.
    Crystal structures of thermally stable adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis (2014), J. Korean Soc. Appl. Biol. Chem., 57, 661-665.
No PubMed abstract available
Search for more literature for 2.7.4.3

Cloned(Commentary)

Cloned (Comment) Organism
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli Bacillus subtilis
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli Geobacillus stearothermophilus
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli Sporosarcina globispora

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively Bacillus subtilis
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively Geobacillus stearothermophilus
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively Sporosarcina globispora

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview Bacillus subtilis
additional information construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview Geobacillus stearothermophilus
additional information construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview Sporosarcina globispora

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P16304 gene adk
-
Bacillus subtilis 168 P16304 gene adk
-
Geobacillus stearothermophilus P27142 gene adk
-
Sporosarcina globispora P84139 gene adk
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged mutant AKm1 and AKm2 enzymes from Escherichia coli by nickel affinity chromatography and gel filtration Bacillus subtilis
recombinant His-tagged mutant AKm1 and AKm2 enzymes from Escherichia coli by nickel affinity chromatography and gel filtration Geobacillus stearothermophilus
recombinant His-tagged mutant AKm1 and AKm2 enzymes from Escherichia coli by nickel affinity chromatography and gel filtration Sporosarcina globispora

Synonyms

Synonyms Comment Organism
AKlse4
-
 Bacillus subtilis
AKmeso
-
 Bacillus subtilis
AKpsycrho
-
 Sporosarcina globispora
AKthermo
-
 Geobacillus stearothermophilus

General Information

General Information Comment Organism
additional information optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2 Bacillus subtilis
additional information optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2 Geobacillus stearothermophilus
additional information optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2 Sporosarcina globispora