2e1b
From Proteopedia
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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: | + | [[Category: National project on protein structural and functional analyse]] |
- | [[Category: | + | [[Category: Nppsfa]] |
- | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
- | [[Category: | + | [[Category: Rsgi]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Trans-editing enzyme]] |
- | [[Category: | + | [[Category: Zinc-binding motif]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:44:42 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 22:44, 3 May 2008
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
Categories: Pyrococcus horikoshii | Single protein | Fukunaga, R. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Trans-editing enzyme | Zinc-binding motif