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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-10, Vol.66 (10), p.1326-1334
• Main Authors: 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: Article
• Language: English
• Subjects: 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
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309110037619

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.