Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop
- 15 January 2012
- journal article
- Published by Elsevier BV in Archives of Biochemistry and Biophysics
- Vol. 517 (2), 111-122
- https://doi.org/10.1016/j.abb.2011.11.017
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Features and development of CootActa crystallographica. Section D, Structural biology, 2010
- Structural Basis for the Altered Activity of Gly794 Variants of Escherichia coli β-Galactosidase†Biochemistry, 2003
- His-357 of β-Galactosidase (Escherichia coli) Interacts with the C3 Hydroxyl in the Transition State and Helps To Mediate CatalysisBiochemistry, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa crystallographica. Section D, Structural biology, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- The β-Galactosidase ( ) Reaction Is Partly Facilitated by Interactions of His-540 with the C6 Hydroxyl of GalactoseOnline Journal of Public Health Informatics, 1996
- GLU-416 of β-Galactosidase (Escherichia coli) Is a MG2+Ligand and β-Galactosidases with Substitutions for GLU-416 Are Inactivated, Rather than Activated, by MG2+Biochemical and Biophysical Research Communications, 1996
- The CCP4 suite: programs for protein crystallographyActa crystallographica. Section D, Structural biology, 1994
- Substitutions for Gly-794 show that binding interactions are important determinants of the catalytic action of β-galactosidase (Escherichia coli)Biochemistry and Cell Biology, 1994
- Genetic regulatory mechanisms in the synthesis of proteinsJournal of Molecular Biology, 1961