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2e1b

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|PDB= 2e1b |SIZE=350|CAPTION= <scene name='initialview01'>2e1b</scene>, resolution 2.70&Aring;
|PDB= 2e1b |SIZE=350|CAPTION= <scene name='initialview01'>2e1b</scene>, resolution 2.70&Aring;
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY=
|GENE=
|GENE=
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|RELATEDENTRY=
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|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.]]
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[[Category: ZN]]
 
[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:34:00 2008''
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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 23:42, 30 March 2008


PDB ID 2e1b

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands:
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

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