Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan

Madhavan R Buddha; Brian R Crane

doi:10.1038/nsmb907

Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan

Nat Struct Mol Biol. 2005 Mar;12(3):274-5. doi: 10.1038/nsmb907. Epub 2005 Feb 20.

Authors

Madhavan R Buddha¹, Brian R Crane

Affiliation

¹ Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA.

PMID: 15723076
DOI: 10.1038/nsmb907

Abstract

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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

5-Hydroxytryptophan / metabolism
Catalysis
Crystallography
Deinococcus / enzymology
Molecular Structure
Nitric Oxide / metabolism
RNA, Transfer, Trp / metabolism*
Substrate Specificity
Tryptophan / analogs & derivatives*
Tryptophan / metabolism*
Tryptophan-tRNA Ligase / chemistry*
Tryptophan-tRNA Ligase / metabolism*

Substances

4-nitro-tryptophan
RNA, Transfer, Trp
Nitric Oxide
Tryptophan
5-Hydroxytryptophan
Tryptophan-tRNA Ligase