Crystal structure of a eukaryote/archaeon-like protyl-tRNA synthetase and its complex with tRNAPro(CGG).

ABSTRACT: 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 angstom 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 tRNAP

SUBMITTER: Yaremchuk A 

PROVIDER: S-EPMC302085 | biostudies-literature | 2000 Sep

REPOSITORIES: biostudies-literature