2e1b: Difference between revisions

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{{STRUCTURE_2e1b|  PDB=2e1b  |  SCENE=  }}  
{{STRUCTURE_2e1b|  PDB=2e1b  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17327676}}


==About this Structure==
==About this Structure==
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[[Category: Trans-editing enzyme]]
[[Category: Trans-editing enzyme]]
[[Category: Zinc-binding motif]]
[[Category: Zinc-binding motif]]
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Revision as of 08:46, 29 July 2008

File:2e1b.png

Template:STRUCTURE 2e1b

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

Template:ABSTRACT PUBMED 17327676

About this Structure

2E1B is a Single protein structure of sequence from Pyrococcus horikoshii. 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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