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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 DOI10.2210/pdb2g36/pdb
DescriptorTryptophanyl-tRNA synthetase, IRON/SULFUR CLUSTER, TRYPTOPHAN, ... (4 entities in total)
Functional Keywordstm0492, 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 sourceThermotoga maritima
Cellular locationCytoplasm : Q9WYW2
Total number of polymer chains1
Total formula weight39840.05
Authors
Joint Center for Structural Genomics (JCSG) (deposition date: 2006-02-17, release date: 2006-03-28, Last modification date: 2024-04-03)
Primary citationHan, 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: 20944229
DOI: 10.1107/S1744309110037619
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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