1ob0
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KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE
OverviewOverview
It is generally assumed that in proteins hydrophobic residues are not, favorable at solvent-exposed sites, and that amino acid substitutions on, the surface have little effect on protein thermostability. Contrary to, these assumptions, we have identified hyperthermostable variants of, Bacillus licheniformis alpha-amylase (BLA) that result from the, incorporation of hydrophobic residues at the surface. Under highly, destabilizing conditions, a variant combining five stabilizing mutations, unfolds 32 times more slowly and at a temperature 13 degrees C higher than, the wild-type. Crystal structure analysis at 1.7 A resolution suggests, that stabilization is achieved through (a) extension of the concept of, increased hydrophobic packing, usually applied to cavities, to surface, indentations, ... [(full description)]
About this StructureAbout this Structure
1OB0 is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA and NA as [ligands]. Active as [[1]], with EC number [3.2.1.1]. Full crystallographic information is available from [OCA].
ReferenceReference
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface., Machius M, Declerck N, Huber R, Wiegand G, J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:12540849
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