6j7c

Crystal structure of proline racemase-like protein from Thermococcus litoralis in complex with proline

spinqualitylabelsall models 6j7c, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j7c is a 1 chain structure with sequence from Theln. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PRO Gene: OCC_00372 (THELN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 2.7A 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. Crystal structure of substrate-bound bifunctional proline racemase/hydroxyproline epimerase from a hyperthermophilic archaeon.,Watanabe Y, Watanabe S, Itoh Y, Watanabe Y Biochem Biophys Res Commun. 2019 Mar 26;511(1):135-140. doi:, 10.1016/j.bbrc.2019.01.141. Epub 2019 Feb 14. PMID:30773259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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