Mycobacterium tuberculosis Strains Possess Functional Cellulases

A. Varrott, S. Leydiert, G. Pell, J.M. Macdonald, Robert Stick, B. Henrissat, H.J. Gilbert, G.J. Davies

Research output: Contribution to journalArticlepeer-review

51 Citations (Scopus)


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 1.1 angstrom 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.
Original languageEnglish
Pages (from-to)20181-20184
JournalJournal of Biological Chemistry
Issue number21
Publication statusPublished - 2005


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