1UP2
Structure of the endoglucanase Cel6 from Mycobacterium tuberculosis in complex with glucose-isofagomine at 1.9 angstrom
Summary for 1UP2
| Entry DOI | 10.2210/pdb1up2/pdb |
| Related | 1UOZ 1UP0 1UP3 1UP4 1UP6 1UP7 |
| Descriptor | CELA1 PROTEIN, 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE, beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | hydrolase, glycoside hydrolase, family 6 |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 31799.83 |
| 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: 2024-10-23) |
| Primary citation | Varrot, 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: 15824123DOI: 10.1074/JBC.C500142200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
