5Y33

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

Summary for 5Y33

Entry DOI	10.2210/pdb5y33/pdb
Descriptor	Alginate lyase (2 entities in total)
Functional Keywords	alginate lyase, b-elimination reaction, b-jelly roll fold, endolytic enzyme, structural protein
Biological source	Flavobacterium sp. UMI-01
Total number of polymer chains	1
Total formula weight	29901.76
Authors	Qin, H.-M.,Miyakawa, T.,Nakamura, A.,Tanokura, M. (deposition date: 2017-07-27, release date: 2018-07-04, Last modification date: 2024-03-27)
Primary citation	Qin, H.M.,Miyakawa, T.,Inoue, A.,Nishiyama, R.,Nakamura, A.,Asano, A.,Ojima, T.,Tanokura, M. Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family. Chem. Commun. (Camb.), 54:555-558, 2018 Cited by PubMed Abstract: 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. PubMed: 29292806 DOI: 10.1039/c7cc06523j PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.54 Å)

Structure validation