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

The structure of the thermostable triosephosphate isomerase (TIM) from Bacillus stearothermophilus complexed with the competitive inhibitor 2‐phosphoglycolate was determined by X‐ray crystallography to a resolution of 2.8 A. The structure was solved by molecular replacement using XPLOR. Twofold aver...

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Veröffentlicht in:	Protein science 1995-12, Vol.4 (12), p.2594-604
Hauptverfasser:	Delboni, Luis F, Mande, Shekhar C, Rentier-Delrue, Françoise, Mainfroid, Véronique, Turley, Stewart, Vellieux, Frederique M D, Martial, Joseph, Hol, WIM G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus stearothermophilus/enzymology Binding Sites Binding, Competitive Biochemistry Biochemistry, biophysics & molecular biology Biochimie, biophysique & biologie moléculaire biophysics Chemical Phenomena Chemistry, Physical Crystallization Crystallography, X-Ray Enzyme Inhibitors - metabolism Enzyme Stability Geobacillus stearothermophilus - enzymology Glycolates - metabolism Hot Temperature Hydrogen Bonding hydrophobicity Life sciences Models, Molecular molecular biology Molecular Sequence Data Molecular Structure Physicochemical Phenomena Proline - chemistry Recombinant Proteins - chemistry Sciences du vivant Structure-Activity Relationship thermostability Triose-Phosphate Isomerase - antagonists & inhibitors Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - metabolism Triose-Phosphate Isomerase/antagonists & inhibitors/chemistry/metabolism triosephosphate isomerase
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