1up2
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE ENDOGLUCANASE CEL6 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH GLUCOSE-ISOFAGOMINE AT 1.9 ANGSTROM
Overview
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.
About this Structure
1UP2 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Mycobacterium tuberculosis strains possess functional cellulases., Varrot A, Leydier S, Pell G, Macdonald JM, Stick RV, Henrissat B, Gilbert HJ, Davies GJ, J Biol Chem. 2005 May 27;280(21):20181-4. Epub 2005 Apr 11. PMID:15824123
Page seeded by OCA on Mon Mar 31 00:13:21 2008
