1AH2

SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES

Summary for 1AH2

• Entry DOI: 10.2210/pdb1ah2/pdb
• Descriptor: SERINE PROTEASE PB92 (1 entity in total)
• Functional Keywords: serine protease, subtilase, industrial enzyme, maxacal(tm), application in washing powders
• Biological source: Bacillus alcalophilus
• Cellular location: Secreted: P27693
• Total number of polymer chains: 1
• Total formula weight: 26745.41

Authors

Boelens, R.,Schipper, D.,Martin, J.R.,Karimi-Nejad, Y.,Mulder, F.,Zwan, J.V.D.,Mariani, M. (deposition date: 1997-04-11, release date: 1998-04-15, Last modification date: 2024-05-22)

Primary citation

Martin, J.R.,Mulder, F.A.,Karimi-Nejad, Y.,van der Zwan, J.,Mariani, M.,Schipper, D.,Boelens, R.
The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.
Structure, 5:521-532, 1997

PubMed Abstract: 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 provide further details about the conformation of this key region and give new insights into the functional properties of these enzymes.

PubMed: 9115441
DOI: 10.1016/S0969-2126(97)00208-6

Experimental method

SOLUTION NMR