1ak9

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spinqualitylabelsall models 1ak9, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SUBTILISIN MUTANT 8321

Overview

Six individual amino acid substitutions at separate positions in the, tertiary structure of subtilisin BPN' (EC 3.4.21.14) were found to, increase the stability of this enzyme, as judged by differential scanning, calorimetry and decreased rates of thermal inactivation. These stabilizing, changes, N218S, G169A, Y217K, M50F, Q206C, and N76D, were discovered, through the use of five different investigative approaches: (1) random, mutagenesis; (2) design of buried hydrophobic side groups; (3) design of, electrostatic interactions at Ca2+ binding sites; (4) sequence homology, consensus; and (5) serendipity. Individually, the six amino acid, substitutions increase the delta G of unfolding between 0.3 and 1.3, kcal/mol at 58.5 degrees C. The combination of these six individual, stabilizing ... [(full description)]

About this Structure

1AK9 is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA, NA and IPA as [ligands]. Active as [[1]], with EC number [3.4.21.62]. Full crystallographic information is available from [OCA].

Reference

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:2684274

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