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1UOZ

Structure of the endoglucanase Cel6 from Mycobacterium tuberculosis in complex with thiocellopentaose at 1.1 angstrom

Summary for 1UOZ
Entry DOI10.2210/pdb1uoz/pdb
Related1UP0 1UP2 1UP3 1UP4 1UP6 1UP7
DescriptorPUTATIVE CELLULASE, alpha-D-glucopyranose-(1-4)-1,4-dithio-beta-D-glucopyranose-(1-4)-1,4-dithio-beta-D-glucopyranose, 4-thio-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordshydrolase, glycoside hydrolase, family 6
Biological sourceMYCOBACTERIUM TUBERCULOSIS
Total number of polymer chains1
Total formula weight34129.56
Authors
Varrot, A.,Leydier, S.,Pell, G.,Gilbert, H.J.,Davies, G.J. (deposition date: 2003-09-26, release date: 2004-11-18, Last modification date: 2024-10-16)
Primary citationVarrot, A.,Leydier, S.,Pell, G.,Macdonald, J.M.,Stick, R.V.,Henrissat, B.,Gilbert, H.J.,Davies, G.J.
Mycobacterium Tuberculosis Strains Possess Functional Cellulases.
J.Biol.Chem., 280:20181-, 2005
Cited by
PubMed 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 1.1A 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.
PubMed: 15824123
DOI: 10.1074/JBC.C500142200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.1 Å)
Structure validation

227561

數據於2024-11-20公開中

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