Structural highlights
Publication Abstract from PubMed
The protein Smu.1393c from Streptococcus mutans is annotated as a putative alpha/beta hydrolase, but it has low sequence identity to the structure-known alpha/beta hydrolases. Here we present the crystal structure of Smu.1393c at 2.0 A 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. Proteins 2013; (c) 2013 Wiley Periodicals, Inc.
Structural and functional characterization of a novel alpha/beta hydrolase from cariogenic pathogen Streptococcus mutans.,Wang Z, Li L, Su XD Proteins. 2013 Sep 30. doi: 10.1002/prot.24418. PMID:24115105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang Z, Li L, Su XD. Structural and functional characterization of a novel alpha/beta hydrolase from cariogenic pathogen Streptococcus mutans. Proteins. 2013 Sep 30. doi: 10.1002/prot.24418. PMID:24115105 doi:http://dx.doi.org/10.1002/prot.24418
