Structural Studies of Lysyl-tRNA Synthetase: Conformational Changes Induced by Substrate Binding
- 26 September 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (42) , 12853-12861
- https://doi.org/10.1021/bi001487r
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogueThe EMBO Journal, 2000
- Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific featuresJournal of Molecular Biology, 1999
- The Structure of Threonyl-tRNA Synthetase-tRNAThr Complex Enlightens Its Repressor Activity and Reveals an Essential Zinc Ion in the Active SiteCell, 1999
- The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acidThe EMBO Journal, 1998
- Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.The EMBO Journal, 1995
- Comparison of the Enzymatic Properties of the Two Escherichia coli Lysyl-tRNA Synthetase SpeciesJournal of Biological Chemistry, 1995
- Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetasePublished by Elsevier ,1995
- Escherichia coli leucine‐responsive regulatory protein (Lrp) controls lysyl‐tRNA synthetase expressionFEBS Letters, 1992
- Control of Escherichia coli lysyl-tRNA synthetase expression by anaerobiosisJournal of Bacteriology, 1991
- Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolutionJournal of Molecular Biology, 1989