| Title : Structural and functional characterization of a novel alpha\/beta hydrolase from cariogenic pathogen Streptococcus mutans - Wang_2014_Proteins_82_695 |
| Author(s) : Wang Z , Li L , Su XD |
| Ref : Proteins , 82 :695 , 2014 |
| Abstract : 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 2014; 82:695-700. (c) 2013 Wiley Periodicals, Inc. |
| ESTHER : Wang_2014_Proteins_82_695 |
| PubMedSearch : Wang_2014_Proteins_82_695 |
| PubMedID: 24115105 |
| Gene_locus related to this paper: strmu-SMU.1393C |
| Gene_locus related to this paper: strmu-SMU.1393C |
Wang Z, Li L, Su XD (2014)
Structural and functional characterization of a novel alpha\/beta hydrolase from cariogenic pathogen Streptococcus mutans
Proteins
82 :695
Wang Z, Li L, Su XD (2014)
Proteins
82 :695