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spinqualitylabelsall models 2e1b, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii

Overview

The editing domain of alanyl-tRNA synthetase (AlaRS) contributes to, high-fidelity aminoacylation by hydrolyzing (editing) the incorrect, products Ser-tRNA(Ala) and Gly-tRNA(Ala) (cis-editing). The AlaX protein, shares sequence homology to the editing domain of AlaRS. There are three, types of AlaX proteins, with different numbers of amino-acid residues, (AlaX-S, AlaX-M and AlaX-L). In this report, AlaX-M from Pyrococcus, horikoshii is shown to deacylate Ser-tRNA(Ala) and Gly-tRNA(Ala), (trans-editing). The crystal structure of P. horikoshii AlaX-M has been, determined at 2.7 A resolution. AlaX-M consists of an N-terminal domain, (N-domain) and a C-terminal domain (C-domain). A zinc ion is coordinated, by the conserved zinc-binding cluster in the C-domain, which is expected, to be the enzymatic active site. The glycine-rich motif, consisting of, successive conserved glycine residues in the N-domain, forms a loop (the, ;glycine-rich loop'). The glycine-rich loop is located near the active, site and may be involved in substrate recognition and/or catalysis.

About this Structure

2E1B is a Single protein structure of sequence from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii., Fukunaga R, Yokoyama S, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):390-400. Epub 2007, Feb 21. PMID:17327676

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