1WLE

Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate

Summary for 1WLE

• Entry DOI: 10.2210/pdb1wle/pdb
• Descriptor: Seryl-tRNA synthetase, SERYL ADENYLATE (3 entities in total)
• Functional Keywords: ligase
• Biological source: Bos taurus (cattle)
• Cellular location: Mitochondrion matrix: Q9N0F3
• Total number of polymer chains: 2
• Total formula weight: 113994.69

Authors

Chimnaronk, S.,Jeppesen, M.G.,Suzuki, T.,Nyborg, J.,Watanabe, K. (deposition date: 2004-06-25, release date: 2005-09-06, Last modification date: 2023-10-25)

Primary citation

Chimnaronk, S.,Jeppesen, M.G.,Suzuki, T.,Nyborg, J.,Watanabe, K.
Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria
Embo J., 24:3369-3379, 2005

PubMed Abstract: 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.

PubMed: 16163389
DOI: 10.1038/sj.emboj.7600811

Experimental method

X-RAY DIFFRACTION (1.65 Å)