comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
enzyme forms binary complex with aminoacyl-tRNA synthetase like protein YbaK and ternary complexes with YbaK and tRNA. Specificity of trans-editing by YbaK is ensured through formation of complexes
the human EPRS consists of four major domains: an N-terminal elongation factor-1Bgamma-like domain, an ERS catalytic domain, a 300 amino acid linker domain containing three tandem WHEP domains, and a C-terminal PRS catalytic domain
the largest subunit (MW 150000, by SDS-PAGE) of the mammalian high-MW complex may be a bifunctional protein exhibiting both glutamyl-tRNA synthetase and prolyl-tRNA synthetase activities
enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure that can be visualized by electron microscopy
the enzyme possess motifs for a catalytic, an anti-codon binding and a tRNA editing activity, similar to the ones found in the canonical prolyl-tRNA synthetase of Escherichia coli and Mycobacterium tuberculosis
the enzyme possess motifs for a catalytic, an anti-codon binding and a tRNA editing activity, similar to the ones found in the canonical prolyl-tRNA synthetase of Escherichia coli and Mycobacterium tuberculosis
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, cognate and noncognate adenylate analogue complexes, overview
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, cognate and noncognate adenylate analogue complexes, overview