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PDBsum entry 6j7c
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References listed in PDB file
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Key reference
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Title
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Crystal structure of substrate-Bound bifunctional proline racemase/hydroxyproline epimerase from a hyperthermophilic archaeon.
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Authors
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Y.Watanabe,
S.Watanabe,
Y.Itoh,
Y.Watanabe.
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Ref.
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Biochem Biophys Res Commun, 2019,
511,
135-140.
[DOI no: ]
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PubMed id
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Abstract
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The hypothetical OCC_00372 protein from Thermococcus litoralis is a member of
the ProR superfamily from hyperthermophilic archaea and exhibits unique
bifunctional proline racemase/hydroxyproline 2-epimerase activity. However, the
molecular mechanism of the broad substrate specificity and extreme
thermostability of this enzyme (TlProR) remains unclear. Here we determined the
crystal structure of TlProR at 2.7 Å resolution. Of note, a substrate proline
molecule, derived from expression host Escherichia coli cells, was tightly bound
in the active site of TlProR. The substrate bound structure and mutational
analyses suggested that Trp241 is involved in hydroxyproline recognition by
making a hydrogen bond between the indole group of Trp241 and the hydroxyl group
of hydroxyproline. Additionally, Tyr171 may contribute to the thermostability by
making hydrogen bonds between the hydroxyl group of Tyr171 and catalytic
residues. Our structural and functional analyses provide a structural basis for
understanding the molecular mechanism of substrate specificity and
thermostability of ProR superfamily proteins.
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