Role of invariant water molecules and water-mediated ionic interactions in D-xylose isomerase fromStreptomyces rubiginosus
| Autor: | Devadasan Velmurugan, V Dhanasekaran, Shankar Prasad Kanaujia, Kanagaraj Sekar |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Xylose isomerase Protein Conformation Stereochemistry Molecular Conformation Ionic bonding Isomerase Crystallography X-Ray Protein structure Bacterial Proteins Structural Biology Molecule Binding site Molecular Biology Aldose-Ketose Isomerases Ions chemistry.chemical_classification Binding Sites Water General Medicine Streptomyces Protein Structure Tertiary Enzyme chemistry Streptomyces rubiginosus Protein Binding |
| Zdroj: | Journal of Biomolecular Structure and Dynamics. 31:376-384 |
| ISSN: | 1538-0254 0739-1102 |
| DOI: | 10.1080/07391102.2012.703064 |
| Popis: | The enzyme, D-xylose isomerase (D-xylose keto-isomerase; EC 5.3.1.5) is a soluble enzyme that catalyzes the conversion of the aldo-sugar D-xylose to the keto-sugar D-xylulose. A total of 27 subunits of D-xylose isomerase from Streptomyces rubiginosus were analyzed in order to identify the invariant water molecules and their water-mediated ionic interactions. A total of 70 water molecules were found to be invariant. The structural and/or functional roles of these water molecules have been discussed. These invariant water molecules and their ionic interactions may be involved in maintaining the structural stability of the enzyme D-xylose isomerase. Fifty-eight of the 70 invariant water molecules (83%) have at least one interaction with the main chain polar atom. |
| Databáze: | OpenAIRE |
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