Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants
| Autor: | James A. Brannigan, Cheravakkattu G. Suresh, Archana Pundle, P.M. Chandra, Guy Dodson, Asmita Prabhune, Johan P. Turkenburg |
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| Rok vydání: | 2004 |
| Předmět: |
Mutant
Biophysics Bacillus Penicillin amidase medicine.disease_cause Biochemistry Bacillus sphaericus law.invention Bacterial Proteins Structural Biology law Escherichia coli Genetics medicine Cloning Molecular chemistry.chemical_classification Cloning integumentary system biology fungi Condensed Matter Physics biology.organism_classification Recombinant Proteins Crystallography Enzyme Amino Acid Substitution chemistry Crystallization Communications Mutagenesis Site-Directed Recombinant DNA Penicillin Amidase Crystallization Monoclinic crystal system |
| Zdroj: | Europe PubMed Central |
| ISSN: | 1744-3091 |
| Popis: | The crystallization of three catalytically inactive mutants of penicillin V acylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme. |
| Databáze: | OpenAIRE |
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