The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3

J Biol Chem. 1998 Dec 11;273(50):33572-9. doi: 10.1074/jbc.273.50.33572.


The soil-dwelling microbe, Pseudomonas sp. strain CBS-3, has attracted recent attention due to its ability to survive on 4-chlorobenzoate as its sole carbon source. The biochemical pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate consists of three enzymes: 4-chlorobenzoyl-CoA ligase, 4-chlorobenzoyl-CoA dehalogenase, and 4-hydroxybenzoyl-CoA thioesterase. Here we describe the three-dimensional structure of the thioesterase determined to 2.0-A resolution. Each subunit of the homotetramer is characterized by a five-stranded anti-parallel beta-sheet and three major alpha-helices. While previous amino acid sequence analyses failed to reveal any similarity between this thioesterase and other known proteins, the results from this study clearly demonstrate that the molecular architecture of 4-hydroxybenzoyl-CoA thioesterase is topologically equivalent to that observed for beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. On the basis of the structural similarity between these two enzymes, the active site of the thioesterase has been identified and a catalytic mechanism proposed.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Aspartic Acid / chemistry
  • Aspartic Acid / metabolism
  • Binding Sites
  • Catalysis
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Pseudomonas / enzymology*
  • Sequence Homology, Amino Acid
  • Thiolester Hydrolases / chemistry*
  • Thiolester Hydrolases / metabolism


  • Aspartic Acid
  • 4-hydroxybenzoyl-CoA hydrolase
  • Thiolester Hydrolases

Associated data

  • PDB/1BVQ