Abstract
The protein Smu.1393c from Streptococcus mutans is annotated as a putative α/β hydrolase, but it has low sequence identity to the structure-known α/β hydrolases. Here we present the crystal structure of Smu.1393c at 2.0 Å resolution. Smu.1393c has a fully open alkaline substrate pocket, whose conformation is unique among other similar hydrolase structures. Three residues, Ser101, His251, and Glu125, were identified as the active center of Smu.1393c. By screening a series of artificial hydrolase substrates, we demonstrated Smu.1393c had low carboxylesterase activity towards short-chain carboxyl esters, which provided a clue for exploring the in vivo function of Smu.1393c.
Original language | English (US) |
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Pages (from-to) | 695-700 |
Number of pages | 6 |
Journal | Proteins: Structure, Function and Bioinformatics |
Volume | 82 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2014 |
Externally published | Yes |
Keywords
- Cap domain
- Carboxylesterase
- Catalytic triad
- Smu.1393c
- X-ray crystallography
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology