Structural and functional characterization of a novel α/β hydrolase from cariogenic pathogen Streptococcus mutans

Zixi Wang, Lanfen Li, Xiao Dong Su

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)695-700
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Volume82
Issue number4
DOIs
StatePublished - Apr 2014
Externally publishedYes

Keywords

  • Cap domain
  • Carboxylesterase
  • Catalytic triad
  • Smu.1393c
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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