Structural Snapshots of the KMSKS Loop Rearrangement for Amino Acid Activation by Bacterial Tyrosyl-tRNA Synthetase
- 11 February 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 346 (1), 105-117
- https://doi.org/10.1016/j.jmb.2004.11.034
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
- RIKEN
This publication has 43 references indexed in Scilit:
- Interconversion of ATP Binding and Conformational Free Energies by Tryptophanyl-tRNA Synthetase: Structures of ATP Bound to Open and Closed, Pre-Transition-state ConformationsJournal of Molecular Biology, 2002
- Comparison of the Catalytic Roles Played by the KMSKS Motif in the Human and Bacillus stearothermophilus Tyrosyl-tRNA SynthetasesPublished by Elsevier ,2002
- ESPript: analysis of multiple sequence alignments in PostScript.Bioinformatics, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- Analysis of the Role of the KMSKS Loop in the Catalytic Mechanism of the Tyrosyl-tRNA Synthetase Using Multimutant CyclesBiochemistry, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetaseBiochemistry, 1993
- Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsNature, 1990
- Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolutionJournal of Molecular Biology, 1989
- Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosineJournal of Molecular Biology, 1987