The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates

FEBS Lett. 2014 Mar 18;588(6):995-1000. doi: 10.1016/j.febslet.2014.01.060. Epub 2014 Feb 11.

Abstract

VinJ is an amidohydrolase belonging to the serine peptidase family that catalyzes the hydrolysis of the terminal aminoacyl moiety of a polyketide intermediate during the biosynthesis of vicenistatin. Herein, we report the crystal structure of VinJ. VinJ possesses a unique hydrophobic tunnel for the recognition of the polyketide chain moiety of its substrate in the cap domain. Taken together with the results of phylogenetic analysis, our results suggest that VinJ represents a new amidohydrolase family that is different from the known α/β hydrolase type serine peptidases.

Keywords: Amidohydrolase; Biosynthesis; Crystal structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / genetics
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Catalytic Domain
  • Conserved Sequence
  • Crystallography, X-Ray
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Polyketides / chemistry*
  • Protein Binding
  • Protein Structure, Secondary
  • Streptomyces / enzymology*

Substances

  • Bacterial Proteins
  • Polyketides
  • Amidohydrolases