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- Title
An Inserted &agr;/&bgr; Subdomain Shapes the Catalytic Pocket of Lactobacillus johnsonii Cinnamoyl Esterase.
- Authors
Kin-Kwan Lai; Stogios, Peter J.; Clara Vu; Xiaohui Xu; Hong Cui; Molloy, Sara; Savchenko, Alexei; Yakunin, Alexander; Gonzalez, Claudio F.
- Abstract
Background: Microbial enzymes produced in the gastrointestinal tract are primarily responsible for the release and biochemical transformation of absorbable bioactive monophenols. In the present work we described the crystal structure of LJ0536, a serine cinnamoyl esterase produced by the probiotic bacterium Lactobacillus johnsonii N6.2. Methodology/Principal Findings: We crystallized LJ0536 in the apo form and in three substrate-bound complexes. The structure showed a canonical &agr;/&bgr;fold characteristic of esterases, and the enzyme is dimeric. Two classical serine esterase motifs (GlyXSerXGly) can be recognized from the amino acid sequence, and the structure revealed that the catalytic triad of the enzyme is formed by Ser106, His225, and Asp197, while the other motif is non-functional. In all substrate-bound complexes, the aromatic acyl group of the ester compound was bound in the deepest part of the catalytic pocket. The binding pocket also contained an unoccupied area that could accommodate larger ligands. The structure revealed a prominent inserted &agr;/&bgr;subdomain of 54 amino acids, from which multiple contacts to the aromatic acyl groups of the substrates are made. Inserts of this size are seen in other esterases, but the secondary structure topology of this subdomain of LJ0536 is unique to this enzyme and its closest homolog (Est1E) in the Protein Databank. Conclusions: The binding mechanism characterized (involving the inserted &agr;/&bgr; subdomain) clearly differentiates LJ0536 from enzymes with similar activity of a fungal origin. The structural features herein described together with the activity profile of LJ0536 suggest that this enzyme should be clustered in a new group of bacterial cinnamoyl esterases.
- Subjects
LACTOBACILLUS; CINNAMOYL compounds; CATALYTIC activity; MICROBIAL enzymes; GASTROINTESTINAL system; PROBIOTICS; BIOACTIVE compounds; PHENOLS; MICROBIOLOGICAL chemistry; CRYSTALLOGRAPHY
- Publication
PLoS ONE, 2011, Vol 6, Issue 8, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0023269