2e1b: Difference between revisions

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[[Image:2e1b.jpg|left|200px]]
[[Image:2e1b.jpg|left|200px]]


{{Structure
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'''Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii'''
'''Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii'''
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: national project on protein structural and functional analyse]]
[[Category: National project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: Nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: Rsgi]]
[[Category: structural genomic]]
[[Category: Structural genomic]]
[[Category: trans-editing enzyme]]
[[Category: Trans-editing enzyme]]
[[Category: zinc-binding motif]]
[[Category: Zinc-binding motif]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:42:16 2008''

Revision as of 22:44, 3 May 2008

File:2e1b.jpg

Template:STRUCTURE 2e1b

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. 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 Page seeded by OCA on Sun May 4 01:44:42 2008

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