1up2 | pdb_00001up2

STRUCTURE OF THE ENDOGLUCANASE CEL6 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH GLUCOSE-ISOFAGOMINE AT 1.9 ANGSTROM

spinqualitylabelsall models 1up2, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1up2 is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PG, ACT, BGC, IFM, SO4 NonStd Res: MHO Related: 1uoz, 1up0, 1up3, 1up4, 1up6, 1up7 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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