2G36
Crystal structure of Tryptophanyl-tRNA synthetase (EC 6.1.1.2) (Tryptophan-tRNA ligase)(TrpRS) (tm0492) from THERMOTOGA MARITIMA at 2.50 A resolution
Summary for 2G36
| Entry DOI | 10.2210/pdb2g36/pdb |
| Descriptor | Tryptophanyl-tRNA synthetase, IRON/SULFUR CLUSTER, TRYPTOPHAN, ... (4 entities in total) |
| Functional Keywords | tm0492, tryptophanyl-trna synthetase (ec 6.1.1.2) (tryptophan-trna ligase)(trprs), structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi, ligase |
| Biological source | Thermotoga maritima |
| Cellular location | Cytoplasm : Q9WYW2 |
| Total number of polymer chains | 1 |
| Total formula weight | 39840.05 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2006-02-17, release date: 2006-03-28, Last modification date: 2024-04-03) |
| Primary citation | Han, G.W.,Yang, X.L.,McMullan, D.,Chong, Y.E.,Krishna, S.S.,Rife, C.L.,Weekes, D.,Brittain, S.M.,Abdubek, P.,Ambing, E.,Astakhova, T.,Axelrod, H.L.,Carlton, D.,Caruthers, J.,Chiu, H.J.,Clayton, T.,Duan, L.,Feuerhelm, J.,Grant, J.C.,Grzechnik, S.K.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kumar, A.,Marciano, D.,Miller, M.D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Paulsen, J.,Reyes, R.,van den Bedem, H.,White, A.,Wolf, G.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Elsliger, M.A.,Schimmel, P.,Wilson, I.A. Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster. Acta Crystallogr.,Sect.F, 66:1326-1334, 2010 Cited by PubMed Abstract: 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. PubMed: 20944229DOI: 10.1107/S1744309110037619 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report






