4e1y | pdb_00004e1y

Alginate lyase A1-III H192A apo form

spinqualitylabelsall models 4e1y, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e1y is a 2 chain structure with sequence from Sphingomonas sp.. This structure supersedes the now removed PDB entry 3evh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KWU1_SPHSX Publication Abstract from PubMed The structures of two mutants (H192A and Y246F) of a mannuronate-specific alginate lyase, A1-III, from Sphingomonas species A1 complexed with a tetrasaccharide substrate [4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)(2)-mannuronic acid] were determined by X-ray crystallography at around 2.2 A resolution together with the apo form of the H192A mutant. The final models of the complex forms, which comprised two monomers (of 353 amino-acid residues each), 268-287 water molecules and two tetrasaccharide substrates, had R factors of around 0.17. A large conformational change occurred in the position of the lid loop (residues 64-85) in holo H192A and Y246F compared with that in apo H192A. The lid loop migrated about 14 A from an open form to a closed form to interact with the bound tetrasaccharide and a catalytic residue. The tetrasaccharide was bound in the active cleft at subsites -3 to +1 as a substrate form in which the glycosidic linkage to be cleaved existed between subsites -1 and +1. In particular, the O(eta) atom of Tyr68 in the closed lid loop forms a hydrogen bond to the side chain of a presumed catalytic residue, O(eta) of Tyr246, which acts both as an acid and a base catalyst in a syn mechanism. Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III.,Mikami B, Ban M, Suzuki S, Yoon HJ, Miyake O, Yamasaki M, Ogura K, Maruyama Y, Hashimoto W, Murata K Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1207-16. Epub 2012 Aug 18. PMID:22948922 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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