Global Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase A
Open Access
- 1 March 2010
- journal article
- Published by Elsevier BV
- Vol. 285 (13), 9971-9980
- https://doi.org/10.1074/jbc.m109.078717
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- The Thermoplasma acidophilum LplA-LplB Complex Defines a New Class of Bipartite Lipoate-protein LigasesJournal of Biological Chemistry, 2009
- Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA LigaseBiochemistry, 2008
- Inference of Macromolecular Assemblies from Crystalline StateJournal of Molecular Biology, 2007
- Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational ModificationJournal of Molecular Biology, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Electrostatics of nanosystems: Application to microtubules and the ribosomeProceedings of the National Academy of Sciences of the United States of America, 2001
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Studies on Polynucleotides. VII.1 Approaches to the Marking of End Groups in Polynucleotide Chains: The Methylation of Phosphomonoester Groups2Journal of the American Chemical Society, 1959