Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954223/
https://www.ncbi.nlm.nih.gov/pubmed/20944229
http://dx.doi.org/10.1107/S1744309110037619
Descripción
Sumario: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-x (22)-C-x (6)-C-x (2)-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.