1bbw
From Proteopedia
|
LYSYL-TRNA SYNTHETASE (LYSS)
Overview
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.
About this Structure
1BBW is a Single protein structure of sequence from Escherichia coli. Active as Lysine--tRNA ligase, with EC number 6.1.1.6 Full crystallographic information is available from OCA.
Reference
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding., Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P, Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
Page seeded by OCA on Tue Nov 20 11:31:47 2007
