The crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanism
| Autor: | Glaucius Oliva, Maria Amélia Oliva Dotta, Andréia Gianotti, Otavio Henrique Thiemann, Lívia Maria Faim, Flavio Henrique Silva, Ney Ribeiro Leite, Aline Regis Faro |
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| Rok vydání: | 2012 |
| Předmět: |
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Molecular Protein Folding Ribonucleotide Xylellain Biophysics Cysteine Proteinase Inhibitors Crystallography X-Ray Xylella Biochemistry Genome Uridine Diphosphate Mediator Bacterial Proteins Structural Biology Cysteine Proteases Catalytic Domain Hydrolase Genetics Point Mutation Enzyme kinetics Protein Structure Quaternary Molecular Biology Xylella fastidiosa biology Crystal structure Active site Cell Biology biology.organism_classification Cysteine protease Recombinant Proteins Enzyme Activation Kinetics Amino Acid Substitution CRISTALOGRAFIA biology.protein Biocatalysis Mutagenesis Site-Directed Mutant Proteins |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1873-3468 |
| Popis: | Xylella fastidiosa is responsible for a wide range of economically important plant diseases. We report here the crystal structure and kinetic data of Xylellain, the first cysteine protease characterized from the genome of the pathogenic X. fastidiosa strain 9a5c. Xylellain has a papain-family fold, and part of the N-terminal sequence blocks the enzyme active site, thereby mediating protein activity. One novel feature identified in the structure is the presence of a ribonucleotide bound outside the active site. We show that this ribonucleotide plays an important regulatory role in Xylellain enzyme kinetics, possibly functioning as a physiological mediator.Structured summary of protein interactionsXylellain and Xylellain bind by X-ray crystallography (View interaction) |
| Databáze: | OpenAIRE |
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