1bbw
From Proteopedia
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| , resolution 2.7Å | |||||||
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| Gene: | LYSS (Escherichia coli) | ||||||
| Activity: | Lysine--tRNA ligase, with EC number 6.1.1.6 | ||||||
| Related: | 1BBU
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 18:57:46 2008
