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1yi8

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|ACTIVITY=
|ACTIVITY=
|GENE= DR1093 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 Deinococcus radiodurans R1])
|GENE= DR1093 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 Deinococcus radiodurans R1])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yi8 OCA], [http://www.ebi.ac.uk/pdbsum/1yi8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yi8 RCSB]</span>
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[[Category: Buddha, M R.]]
[[Category: Buddha, M R.]]
[[Category: Crane, B R.]]
[[Category: Crane, B R.]]
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[[Category: TRP]]
 
[[Category: auxiliary tryptophanyl trna synthetase]]
[[Category: auxiliary tryptophanyl trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:08:04 2008''

Revision as of 22:08, 30 March 2008


PDB ID 1yi8

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Gene: DR1093 (Deinococcus radiodurans R1)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of tryptophanyl trRNA synthetase II from Deinococcus radiodurans in complex with L-Trp


Overview

The most divergent of two tryptophanyl tRNA synthetases (TrpRS II) found in Deinococcus radiodurans interacts with a nitric oxide synthase protein that produces 4-nitro-tryptophan (4-NRP). TrpRS II efficiently charges transfer RNA(Trp) with 4-NRP and 5-hydroxy-tryptophan (5-HRP). The crystal structures of TrpRS II bound to tryptophan and 5-HRP reveal residue substitutions that accommodate modified indoles. A class of auxiliary bacterial TrpRSs conserve this capacity to charge tRNA with nonstandard amino acids.

About this Structure

1YI8 is a Single protein structure of sequence from Deinococcus radiodurans r1. Full crystallographic information is available from OCA.

Reference

Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan., Buddha MR, Crane BR, Nat Struct Mol Biol. 2005 Mar;12(3):274-5. Epub 2005 Feb 20. PMID:15723076

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