2e1b: Difference between revisions
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|PDB= 2e1b |SIZE=350|CAPTION= <scene name='initialview01'>2e1b</scene>, resolution 2.70Å | |PDB= 2e1b |SIZE=350|CAPTION= <scene name='initialview01'>2e1b</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e1b OCA], [http://www.ebi.ac.uk/pdbsum/2e1b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e1b RCSB]</span> | |||
}} | }} | ||
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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]] | ||
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[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:42:16 2008'' | ||
Revision as of 23:42, 30 March 2008
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| 2e1b, resolution 2.70Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Mon Mar 31 02:42:16 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
