1urx | pdb_00001urx

Crystallographic structure of beta-agarase A in complex with oligoagarose

spinqualitylabelsall models 1urx, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1urx is a 1 chain structure with sequence from "cytophaga_drobachiensis"_barbeyron_et_al._1998 "cytophaga drobachiensis" barbeyron et al. 1998. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AAL, CA, GAL, GLA Activity: Beta-agarase, with EC number 3.2.1.81 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Agarose is a gel-forming polysaccharide with an alpha-L(1,4)-3,6-anhydro-galactose, beta-D(1,3)-galactose repeat unit, from the cell walls of marine red algae. beta-agarase A, from the Gram-negative bacterium Zobellia galactanivorans, is secreted to the external medium and degrades agarose with an endo-mechanism. The structure of the inactive mutant beta-agarase A-E147S in complex with agaro-octaose has been solved at 1.7 A resolution. Two oligosaccharide chains are bound to the protein. The first one resides in the active site channel, spanning subsites -4 to -1. A second oligosaccharide binding site, on the opposite side of the protein, was filled with eight sugar units, parallel to the active site. The crystal structure of the beta-agarase A with agaro-octaose provides detailed information on agarose recognition in the catalytic site. The presence of the second, parallel, binding site suggests that the enzyme might be able to unwind the double-helical structure of agarose prior to the catalytic cleavage. Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose.,Allouch J, Helbert W, Henrissat B, Czjzek M Structure. 2004 Apr;12(4):623-32. PMID:15062085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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