Interconversion of ATP Binding and Conformational Free Energies by Tryptophanyl-tRNA Synthetase: Structures of ATP Bound to Open and Closed, Pre-Transition-state Conformations
- 3 December 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 325 (1), 39-63
- https://doi.org/10.1016/s0022-2836(02)01156-7
Abstract
No abstract availableKeywords
This publication has 76 references indexed in Scilit:
- Correlating amino acid conservation with function in tyrosyl-tRNA synthetaseJournal of Molecular Biology, 2000
- 2.9 Å crystal structure of ligand‐free tryptophanyl‐tRNA synthetase: Domain movements fragment the adenine nucleotide binding siteProtein Science, 2000
- A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetasesBiochimie, 1995
- Analysis of the Role of the KMSKS Loop in the Catalytic Mechanism of the Tyrosyl-tRNA Synthetase Using Multimutant CyclesBiochemistry, 1995
- Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetaseStructure, 1995
- Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetaseBiochemistry, 1993
- Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetaseBiochemistry, 1993
- An operational RNA code for amino acids and possible relationship to genetic code.Proceedings of the National Academy of Sciences, 1993
- COGNITION, MECHANISM, AND EVOLUTIONARY RELATIONSHIPS IN AMINOACYL-tRNA SYNTHETASESAnnual Review of Biochemistry, 1993
- Aminoacyl-tRNA synthetases: Current opinion in structural biology 1992, 2:138…-142Current Opinion in Structural Biology, 1992