6J7C

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

Summary for 6J7C

• Entry DOI: 10.2210/pdb6j7c/pdb
• Descriptor: Proline racemase, PROLINE (3 entities in total)
• Functional Keywords: proline racemase, hydroxyproline 2-epimerase, hyperthermophilic archaea, isomerase
• Biological source: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
• Total number of polymer chains: 1
• Total formula weight: 38316.75

Authors

Watanabe, Y.,Watanabe, S.,Itoh, Y.,Watanabe, Y. (deposition date: 2019-01-17, release date: 2019-02-27, Last modification date: 2023-11-22)

Primary citation

Watanabe, Y.,Watanabe, S.,Itoh, Y.,Watanabe, Y.
Crystal structure of substrate-bound bifunctional proline racemase/hydroxyproline epimerase from a hyperthermophilic archaeon.
Biochem. Biophys. Res. Commun., 511:135-140, 2019

PubMed Abstract: 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.

PubMed: 30773259
DOI: 10.1016/j.bbrc.2019.01.141

Experimental method

X-RAY DIFFRACTION (2.7 Å)