Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity
- 18 May 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 308 (5), 1063-1079
- https://doi.org/10.1006/jmbi.2001.4636
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Structure of the Molybdate/Tungstate Binding Protein Mop from Sporomusa ovataStructure, 2000
- The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain foldsThe EMBO Journal, 1999
- Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 å resolution crystal structure of Azotobacter vinelandii ModAStructure, 1998
- Crystal structure of the molybdate binding protein ModANature Structural & Molecular Biology, 1997
- Characterisation of the Molybdenum‐Responsive ModE Regulatory Protein and its Binding to the Promoter Region of the modABCD (Molybdenum Transport) Operon of Escherichia ColiEuropean Journal of Biochemistry, 1997
- Protein ligands for molybdate. Specificity and charge stabilisation at the anion-binding sites of periplasmic and intracellular molybdate-binding proteins of Azotobacter vinelandii ‡J. Chem. Soc., Dalton Trans., 1997
- High specificity of a phosphate transport protein determined by hydrogen bondsNature, 1990
- Sulfate-binding protein dislikes protonated oxyacidsJournal of Molecular Biology, 1988
- Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bondsNature, 1985
- The Anatomy and Taxonomy of Protein StructureAdvances in protein chemistry, 1981