2nqp

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2nqp, resolution 3.50Å

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Crystal structure of pseudoudirinde synthase TruA in complex with leucyl tRNA

Overview

Translational accuracy and efficiency depend upon modification of uridines, in the tRNA anticodon stem loop (ASL) by a highly conserved pseudouridine, synthase TruA. TruA specifically modifies uridines at positions 38, 39, and/or 40 of tRNAs with highly divergent sequences and structures through, a poorly characterized mechanism that differs from previously studied, RNA-modifying enzymes. The molecular basis for the site and substrate, "promiscuity" was studied by determining the crystal structures of E. coli, TruA in complex with two different leucyl tRNAs in conjunction with, functional assays and computer simulation. The structures capture three, stages of the TruA*tRNA reaction, revealing the mechanism by which TruA, selects the target site. We propose that TruA utilizes the intrinsic, flexibility of the ASL for site promiscuity and also to select against, intrinsically stable tRNAs to avoid their overstabilization through, pseudouridylation, thereby maintaining the balance between the flexibility, and stability required for its biological function.

About this Structure

2NQP is a Protein complex structure of sequences from Escherichia coli with K as ligand. Active as tRNA-pseudouridine synthase I, with EC number 5.4.99.12 Full crystallographic information is available from OCA.

Reference

How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA., Hur S, Stroud RM, Mol Cell. 2007 Apr 27;26(2):189-203. PMID:17466622

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