1wle
From Proteopedia
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Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate
Overview
The secondary structures of metazoan mitochondrial (mt) tRNAs(Ser) deviate, markedly from the paradigm of the canonical cloverleaf structure;, particularly, tRNA(Ser)(GCU) corresponding to the AGY codon (Y=U and C) is, highly truncated and intrinsically missing the entire dihydrouridine arm., None of the mt serine isoacceptors possesses the elongated variable arm, which is the universal landmark for recognition by seryl-tRNA synthetase, (SerRS). Here, we report the crystal structure of mammalian mt SerRS from, Bos taurus in complex with seryl adenylate at an atomic resolution of 1.65, A. Coupling structural information with a tRNA-docking model and the, mutagenesis studies, we have unraveled the key elements that establish, tRNA binding specificity, differ from all other known bacterial and, eukaryotic systems, are the characteristic extensions in both extremities, as well as a few basic residues residing in the amino-terminal helical arm, of mt SerRS. Our data further uncover an unprecedented mechanism of a, dual-mode recognition employed to discriminate two distinct 'bizarre' mt, tRNAs(Ser) by alternative combination of interaction sites.
About this Structure
1WLE is a Single protein structure of sequence from Bos taurus with SRP as ligand. Active as Serine--tRNA ligase, with EC number 6.1.1.11 Full crystallographic information is available from OCA.
Reference
Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria., Chimnaronk S, Gravers Jeppesen M, Suzuki T, Nyborg J, Watanabe K, EMBO J. 2005 Oct 5;24(19):3369-79. Epub 2005 Sep 15. PMID:16163389
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