5y33 | pdb_00005y33

Crystal structure of alginate lyase from Flavobacterium sp. UMI-01 reveals polymannuronate specificity

spinqualitylabelsall models 5y33, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y33 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed FlAlyA is an endolytic enzyme with a preference for polymannuronate. The crystal structure and mutagenesis studies elucidated that the structural variations at outer uronate-binding subsites +2, +3 and -2 control the enzymatic properties of PL-7 family enzymes. Lys158 mutations changed the pH dependency and enhanced the production of mono- and disaccharides. Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family.,Qin HM, Miyakawa T, Inoue A, Nishiyama R, Nakamura A, Asano A, Ojima T, Tanokura M Chem Commun (Camb). 2018 Jan 11;54(5):555-558. doi: 10.1039/c7cc06523j. PMID:29292806 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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