1ah2
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SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES
OverviewOverview
BACKGROUND: Research on high-alkaline proteases, such as serine protease, PB92, has been largely inspired by their industrial application as, protein-degrading components of washing powders. Serine protease PB92 is a, member of the subtilase family of enzymes, which has been extensively, studied. These studies have included exhaustive protein engineering, investigations and X-ray crystallography, in order to provide insight into, the mechanism and specificity of enzyme catalysis. Distortions have been, observed in the substrate-binding region of subtilisin crystal structures, due to crystal contacts. In addition, the structural variability in the, substrate-binding region of subtilisins is often attributed to, flexibility. It was hoped that the solution structure of this enzyme would, ... [(full description)]
About this StructureAbout this Structure
1AH2 is a [Single protein] structure of sequence from [Bacillus alcalophilus]. Full crystallographic information is available from [OCA].
ReferenceReference
The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site., Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R, Structure. 1997 Apr 15;5(4):521-32. PMID:9115441
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