Download MendeleyThe crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli
Onesti, S., Miller, A.D., Brick, P.(1995) Structure 3: 163-176
- PubMed: 7735833
- DOI: https://doi.org/10.1016/s0969-2126(01)00147-2
- Primary Citation of Related Structures:
1LYL - PubMed Abstract:
Lysyl-tRNA synthetase catalyzes the attachment of the amino acid lysine to the cognate tRNA. The enzyme is a member of the class II amino-acyl-tRNA synthetases; the crystal structures of the seryl- and aspartyl-tRNA synthetases from this class are already known. Lysyl-tRNA synthetase shows extensive sequence homology with aspartyl-tRNA synthetase. In Escherichia coli there are two isoforms of the enzyme, LysS and LysU. Unlike LysS, which is synthesized under normal growth conditions, LysU is the product of a normally silent gene which is overexpressed under extreme physiological conditions (such as heat-shock), and can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response.
Organizational Affiliation:
Blackett Laboratory, Imperial College, London, UK.
