1BBW

LYSYL-TRNA SYNTHETASE (LYSS)

Summary for 1BBW

• Entry DOI: 10.2210/pdb1bbw/pdb
• Related: 1BBU
• Descriptor: PROTEIN (LYSYL-TRNA SYNTHETASE) (2 entities in total)
• Functional Keywords: ligase, aminoacyl-trna synthetase, protein biosynthesis
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8N3
• Total number of polymer chains: 1
• Total formula weight: 57546.07

Authors

Onesti, S.,Desogus, G.,Brevet, A.,Chen, J.,Plateau, P.,Blanquet, S.,Brick, P. (deposition date: 1998-04-24, release date: 2000-11-10, Last modification date: 2023-08-09)

Primary citation

Onesti, S.,Desogus, G.,Brevet, A.,Chen, J.,Plateau, P.,Blanquet, S.,Brick, P.
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding.
Biochemistry, 39:12853-12861, 2000

PubMed Abstract: Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.

PubMed: 11041850
DOI: 10.1021/bi001487r

Experimental method

X-RAY DIFFRACTION (2.7 Å)