1LYL

LYSYL-TRNA SYNTHETASE (LYSU) (E.C.6.1.1.6) COMPLEXED WITH LYSINE

Summary for 1LYL

• Entry DOI: 10.2210/pdb1lyl/pdb
• Descriptor: LYSYL-TRNA SYNTHETASE (LYSU), LYSINE (3 entities in total)
• Functional Keywords: ligase (synthetase)
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8N5
• Total number of polymer chains: 3
• Total formula weight: 173743.16

Authors

Onesti, S.,Brick, P. (deposition date: 1995-05-03, release date: 1995-10-15, Last modification date: 2024-02-14)

Primary citation

Onesti, S.,Miller, A.D.,Brick, P.
The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli
Structure, 3:163-176, 1995

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.

PubMed: 7735833
DOI: 10.1016/S0969-2126(01)00147-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)