The crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanism

Autor(es)

Leite, Ney Ribeiro ^[1] ; Faro, Aline Regis ^[1] ; Oliva Dotta, Maria Amelia ^[1] ; Faim, Livia Maria ^[1] ; Gianotti, Andreia ^[2] ; Silva, Flavio Henrique ^[2] ; Oliva, Glaucius ^[1] ; Thiemann, Otavio Henrique ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil

^[2] Univ Fed Sao Carlos, Dept Genet & Evolut, BR-13565905 Sao Carlos, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: FEBS Letters; v. 587, n. 4, p. 339-344, FEB 14 2013.
• Citações Web of Science: 2

Resumo

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 interactions: Xylellain and Xylellain bind by X-ray crystallography (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. (AU)

• Processo FAPESP: 98/14138-2 - Center for Structural Molecular Biotechnology
• Beneficiário: Glaucius Oliva
• Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs