Mycobacterium tuberculosis strains possess functional cellulases

A  Varroto; S  Leydier; G  Pell; J M  Macdonald; R V  Stick; B  Henrissat; H J  Gilbert; G J  Davies

doi:10.1074/jbc.C5000142200

Mycobacterium tuberculosis strains possess functional cellulases

A Varroto, S Leydier, G Pell, J M Macdonald, R V Stick, B Henrissat, H J Gilbert, G J Davies

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	20181-20184
Number of pages	4
Journal	Journal of Biological Chemistry
Volume	280
Issue number	21
DOIs	https://doi.org/10.1074/jbc.C5000142200
Publication status	Published - 27 May 2005

Keywords

PSEUDOMONAS-AERUGINOSA
BINDING
CELLOBIOHYDROLASE
ISOFAGOMINE
REFINEMENT
INHIBITORS
SEQUENCE
DOMAIN
GENES
SUGAR

Access to Document

10.1074/jbc.C5000142200

Cite this

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title = "Mycobacterium tuberculosis strains possess functional cellulases",

abstract = "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.",

keywords = "PSEUDOMONAS-AERUGINOSA, BINDING, CELLOBIOHYDROLASE, ISOFAGOMINE, REFINEMENT, INHIBITORS, SEQUENCE, DOMAIN, GENES, SUGAR",

author = "A Varroto and S Leydier and G Pell and Macdonald, {J M} and Stick, {R V} and B Henrissat and Gilbert, {H J} and Davies, {G J}",

year = "2005",

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doi = "10.1074/jbc.C5000142200",

language = "English",

volume = "280",

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journal = "Journal of Biological Chemistry",

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TY - JOUR

T1 - Mycobacterium tuberculosis strains possess functional cellulases

AU - Varroto, A

AU - Leydier, S

AU - Pell, G

AU - Macdonald, J M

AU - Stick, R V

AU - Henrissat, B

AU - Gilbert, H J

AU - Davies, G J

PY - 2005/5/27

Y1 - 2005/5/27

N2 - 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.

AB - 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.

KW - PSEUDOMONAS-AERUGINOSA

KW - BINDING

KW - CELLOBIOHYDROLASE

KW - ISOFAGOMINE

KW - REFINEMENT

KW - INHIBITORS

KW - SEQUENCE

KW - DOMAIN

KW - GENES

KW - SUGAR

U2 - 10.1074/jbc.C5000142200

DO - 10.1074/jbc.C5000142200

M3 - Article

SN - 0021-9258

VL - 280

SP - 20181

EP - 20184

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 21

ER -