Mycobacterium tuberculosis strains possess functional cellulases
| Autor: | James M. Macdonald, Annabelle Varrot, Sabine Leydier, Gideon J. Davies, Bernard Henrissat, Harry J. Gilbert, Robert V. Stick, Gavin Pell |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular beta-Glucans Cellulase Crystallography X-Ray Biochemistry Catalysis Protein Structure Secondary Substrate Specificity Mycobacterium tuberculosis Protein structure Phylogenetics Polysaccharides Hydrolase Cellulases Binding site Cellulose Molecular Biology Phylogeny Soil Microbiology Binding Sites biology Molecular Structure Cell Biology biology.organism_classification Ligand (biochemistry) biology.protein Crystallization Mycobacterium |
| Zdroj: | The Journal of biological chemistry. 280(21) |
| ISSN: | 0021-9258 |
| Popis: | The genomes of various Mycobacterium tuberculosis strains encode proteins that do not appear to play a role in the growth or survival of the bacterium in its mammalian host, including some implicated in plant cell wall breakdown. Here we show that M. tuberculosis H37Rv does indeed possess a functional cellulase. The x-ray crystal structure of this enzyme, in ligand complex forms, from 1.9 to 1.1A resolution, reveals a highly conserved substrate-binding cleft, which affords similar, and unusual, distortion of the substrate at the catalytic center. The endoglucanase activity, together with the existence of a putative membrane-associated crystalline polysaccharide-binding protein, may reflect the ancestral soil origin of the Mycobacterium or hint at a previously unconsidered environmental niche. |
| Databáze: | OpenAIRE |
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