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PDBsum entry 1bvq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The three-Dimensional structure of 4-Hydroxybenzoyl-Coa thioesterase from pseudomonas sp. Strain cbs-3.
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Authors
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M.M.Benning,
G.Wesenberg,
R.Liu,
K.L.Taylor,
D.Dunaway-Mariano,
H.M.Holden.
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Ref.
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J Biol Chem, 1998,
273,
33572-33579.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Fig. 2. Ribbon representation of one subunit of the
4-hydroxybenzoyl-CoA thioesterase. This figure and Figs. 3-5
were prepared with the software package, MOLSCRIPT (38). The
 -strands are
labeled A-F.
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Figure 4.
Fig. 4. Superposition of the  -carbons
for 4-hydroxybenzoyl-CoA thioesterase and -hydroxydecanoyl
thiol ester dehydrase. X-ray coordinates for the dehydrase were
obtained from the Brookhaven Protein Data Bank (1MKA). The
dehydrase and the thioesterase are displayed in red and black,
respectively. The 3-decynoyl-N-acetylcysteamine suicide
inhibitor observed in the dehydrase structure is depicted in a
ball-and-stick representation.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
33572-33579)
copyright 1998.
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