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Lookup NU author(s): Gavin Pell, Emeritus Professor Harry Gilbert
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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 1.1Å 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. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Author(s): Varrot A, Leydier S, Pell G, Macdonald JM, Stick RV, Henrissat B, Gilbert HJ, Davies GJ
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2005
Volume: 280
Issue: 21
Pages: 20181-20184
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
URL: http://dx.doi.org/10.1074/jbc.C500142200
DOI: 10.1074/jbc.C500142200
PubMed id: 15824123
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