Structure of the multifunctional loops in the nonclassical ATP-binding fold of glutathione synthetase
- 1 January 1996
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 3 (1), 16-18
- https://doi.org/10.1038/nsb0196-16
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Flexible Loop That Is Novel Catalytic Machinery in a Ligase. Atomic Structure and Function of the Loopless Glutathione SynthetaseBiochemistry, 1994
- Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetaseBiochemistry, 1993
- Three-dimensional Structure of the Glutathione Synthetase from Escherichia coli B at 2·0 Å ResolutionJournal of Molecular Biology, 1993
- Use of adenosine(5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli BBiochemistry, 1993
- Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reactionBiochemistry, 1992
- Sequence of a putative glutathione synthetase II gene and flanking regions from Anaplasma centraleBiochemical and Biophysical Research Communications, 1992
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in E. coli methionyl- and valyl-tRNA synthetasesBiochemistry, 1990
- Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal.Biochemistry, 1986
- Complete nucleotide sequence of theE. coliglutathione synthetase gsh-IINucleic Acids Research, 1984