1. The crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanism.
- Author
-
Leite NR, Faro AR, Dotta MA, Faim LM, Gianotti A, Silva FH, Oliva G, and Thiemann OH
- Subjects
- Amino Acid Substitution, Bacterial Proteins agonists, Bacterial Proteins genetics, Bacterial Proteins metabolism, Biocatalysis, Catalytic Domain, Crystallography, X-Ray, Cysteine Proteases genetics, Cysteine Proteases metabolism, Cysteine Proteinase Inhibitors pharmacology, Enzyme Activation, Kinetics, Mutagenesis, Site-Directed, Mutant Proteins agonists, Mutant Proteins antagonists & inhibitors, Mutant Proteins chemistry, Mutant Proteins metabolism, Point Mutation, Protein Folding, Protein Structure, Quaternary, Recombinant Proteins agonists, Recombinant Proteins antagonists & inhibitors, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Uridine Diphosphate chemistry, Uridine Diphosphate metabolism, Bacterial Proteins chemistry, Cysteine Proteases chemistry, Models, Molecular, Xylella enzymology
- Abstract
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., (Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Published
- 2013
- Full Text
- View/download PDF