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| The EMBO Journal
(2000) 19, 4745–4758, doi:10.1093/emboj/19.17.4745 |
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| Crystal structure of a eukaryote/archaeon-like prolyl-tRNA synthetase and its complex with tRNAPro(CGG) |
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| Anna Yaremchuk1, 2, 3, Stephen Cusack1, 3 and Michael Tukalo1, 2 |
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1 European Molecular Biology Laboratory, Grenoble Outstation, c/o ILL, 156X, F-38042 Grenoble Cedex 9, France 2 Instutute of Molecular Biology and Genetics, NAS of Ukraine, 252627 Kiev-143, Ukraine 3 A.yaremchuk and S.Cusack contributed equally to this work To whom correspondence should be addressed Stephen Cusack, cusack@embl-grenoble.fr Michael Tukalo, tukalo@embl-grenoble.fr Received 21 June 2000; Revised 13 July 2000; Accepted 25 July 2000. |
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| Abstract |
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| Prolyl-tRNA synthetase (ProRS) is a class IIa synthetase that, according to sequence analysis, occurs in different organisms with one of two quite distinct structural architectures: prokaryote-like and eukaryote/archaeon-like. The primary sequence of ProRS from the hypothermophilic eubacterium Thermus thermophilus (ProRSTT) shows that this enzyme is surprisingly eukaryote/archaeon-like. We describe its crystal structure at 2.43 Å resolution, which reveals a feature that is unique among class II synthetases. This is an additional zinc-containing domain after the expected class IIa anticodon-binding domain and whose C-terminal extremity, which ends in an absolutely conserved tyrosine, folds back into the active site. We also present an improved structure of ProRSTT complexed with tRNAPro(CGG) at 2.85 Å resolution. This structure represents an initial docking state of the tRNA in which the anticodon stem–loop is engaged, particularly via the tRNAPro-specific bases G35 and G36, but the 3' end does not enter the active site. Considerable structural changes in tRNA and/or synthetase, which are probably induced by small substrates, are required to achieve the conformation active for aminoacylation. |
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| Keywords: anticodon-binding domain, class IIa synthetase, prolyl-tRNA synthetase, tRNA identity, zinc-binding domain |
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