NDLI: Crystal structure of a human aminoacyl-tRNA synthetase cytokine.

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Crystal structure of a human aminoacyl-tRNA synthetase cytokine.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mcree, Duncan E. Skene, Robert J. Yang, Xiang-lei Schimmel, Paul
Description	Author Affiliation: Yang XL ( The Skaggs Institute for Chemical Biology, BCC-379, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.);
Abstract	The 20 aminoacyl-tRNA synthetases catalyze the first step of protein synthesis and establish the rules of the genetic code through aminoacylation reactions. Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase, connect protein synthesis to cell-signaling pathways including angiogenesis. Alternative splicing or proteolysis produces these fragments. The proangiogenic N-terminal fragment mini-TyrRS has IL-8-like cytokine activity that, like other CXC cytokines, depends on a Glu-Leu-Arg motif. Point mutations in this motif abolish cytokine activity. The full-length native TyrRS lacks cytokine activity. No structure has been available for any mammalian tRNA synthetase that, in turn, might give insight into why mini-TyrRS and not TyrRS has cytokine activities. Here, the structure of human mini-TyrRS, which contains both the catalytic and the anticodon recognition domain, is reported to a resolution of 1.18 A. The critical Glu-Leu-Arg motif is located on an internal alpha-helix of the catalytic domain, where the guanidino side chain of R is part of a hydrogen-bonding network tethering the anticodon-recognition domain back to the catalytic site. Whereas the catalytic domains of the human and bacterial enzymes superimpose, the spatial disposition of the anticodon recognition domain relative to the catalytic domain is unique in mini-TyrRS relative to the bacterial orthologs. This unique orientation of the anticodon-recognition domain can explain why the fragment mini-TyrRS, and not full-length native TyrRS, is active in cytokine-signaling pathways.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytokines Chemistry Tyrosine-tRNA Ligase Alternative Splicing Amino Acid Motifs Amino Acid Sequence Anticodon Bacterial Proteins Catalytic Domain Crystallography, X-Ray Physiology Hydrogen Bonding Models, Molecular Molecular Sequence Data Peptide Fragments Protein Conformation Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Species Specificity Structure-Activity Relationship Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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