3OIS

Crystal Structure Xylellain, a cysteine protease from Xylella fastidiosa

Summary for 3OIS

• Entry DOI: 10.2210/pdb3ois/pdb
• Descriptor: Cysteine protease, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: alpha and beta, hydrolase
• Biological source: Xylella fastidiosa
• Total number of polymer chains: 4
• Total formula weight: 133525.16

Authors

Leite, N.R.,Faro, A.R.,Oliva, M.A.V.,Thiemann, O.H.,Oliva, G. (deposition date: 2010-08-19, release date: 2011-08-03, Last modification date: 2024-02-21)

Primary citation

Leite, N.R.,Faro, A.R.,Dotta, M.A.,Faim, L.M.,Gianotti, A.,Silva, F.H.,Oliva, G.,Thiemann, O.H.
The crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanism.
Febs Lett., 587:339-344, 2013

PubMed 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.

PubMed: 23333295
DOI: 10.1016/j.febslet.2013.01.009

Experimental method

X-RAY DIFFRACTION (1.65 Å)