Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster

A novel aminoacyl‐tRNA synthetase that contains an iron–sulfur cluster in the tRNA anticodon‐binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl‐tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron–sulfur [4...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-10, Vol.66 (10), p.1326-1334
Hauptverfasser:	Han, Gye Won, Yang, Xiang-Lei, McMullan, Daniel, Chong, Yeeting E., Krishna, S. Sri, Rife, Christopher L., Weekes, Dana, Brittain, Scott M., Abdubek, Polat, Ambing, Eileen, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Caruthers, Jonathan, Chiu, Hsiu-Ju, Clayton, Thomas, Duan, Lian, Feuerhelm, Julie, Grant, Joanna C., Grzechnik, Slawomir K., Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Kumar, Abhinav, Marciano, David, Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Okach, Linda, Paulsen, Jessica, Reyes, Ron, Van Den Bedem, Henry, White, Aprilfawn, Wolf, Guenter, Xu, Qingping, Hodgson, Keith O., Wooley, John, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., Elsliger, Marc-André, Schimmel, Paul, Wilson, Ian A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Animals BASIC BIOLOGICAL SCIENCES biochemistry & molecular biology biophysics Conserved Sequence Crystal structure crystallography Crystallography, X-Ray Humans iron-sulfur clusters Iron-Sulfur Proteins - chemistry Ligands Ligands That Aid in Function Characterization Models, Molecular Molecular Sequence Data Protein Structure, Quaternary Protein Structure, Tertiary Sequence Alignment structural genomics Thermotoga maritima Thermotoga maritima - enzymology TM0492 Tryptophan-tRNA Ligase - chemistry tryptophanyl-tRNA ligase tryptophanyl-tRNA synthetase class I
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Zusammenfassung:	A novel aminoacyl‐tRNA synthetase that contains an iron–sulfur cluster in the tRNA anticodon‐binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl‐tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron–sulfur [4Fe–4S] cluster bound to the tRNA anticodon‐binding (TAB) domain and an l‐tryptophan ligand in the active site. None of the other T. maritima aminoacyl‐tRNA synthetases (AARSs) contain this [4Fe–4S] cluster‐binding motif (C‐x22‐C‐x6‐C‐x2‐C). It is speculated that the iron–sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.
ISSN:	1744-3091 1744-3091 2053-230X
DOI:	10.1107/S1744309110037619