3afl | pdb_00003afl

Crystal structure of exotype alginate lyase Atu3025 H531A complexed with alginate trisaccharide

spinqualitylabelsall models 3afl, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3afl is a 1 chain structure with sequence from Agrfc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LGU, MAW Related: 3a0o Gene: AGR_L_3558, Atu3025 (AGRFC) 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 Alginate, a major component of the cell wall matrix in brown seaweeds, is degraded by alginate lyases through a beta-elimination reaction. Almost all alginate lyases act endolytically on substrate, thereby yielding unsaturated oligouronic acids having 4-deoxy-l-erythro-hex-4-enepyranosyluronic acid at the nonreducing end. In contrast, Agrobacterium tumefaciens alginate lyase Atu3025, a member of polysaccharide lyase family 15, acts on alginate polysaccharides and oligosaccharides exolytically and releases unsaturated monosaccharides from the substrate terminal. The crystal structures of Atu3025 and its inactive mutant in complex with alginate trisaccharide (H531A/DeltaGGG) were determined at 2.10- and 2.99-A resolutions with final R-factors of 18.3 and 19.9%, respectively, by x-ray crystallography. The enzyme is comprised of an alpha/alpha-barrel + anti-parallel beta-sheet as a basic scaffold, and its structural fold has not been seen in alginate lyases analyzed thus far. The structural analysis of H531A/DeltaGGG and subsequent site-directed mutagenesis studies proposed the enzyme reaction mechanism, with His(311) and Tyr(365) as the catalytic base and acid, respectively. Two structural determinants, i.e. a short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains, are essential for the exolytic mode of action. This is, to our knowledge, the first report on the structure of the family 15 enzyme. Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens.,Ochiai A, Yamasaki M, Mikami B, Hashimoto W, Murata K J Biol Chem. 2010 Aug 6;285(32):24519-28. Epub 2010 May 27. PMID:20507980 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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