1uai
Crystal Structure of the Alginate Lyase from Corynebacterium sp.
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OverviewOverview
The crystal structure of alginate (poly alpha-l-guluronate) lyase from, Corynebacterium sp. (ALY-1) was determined at 1.2A resolution using the, MAD method and bromide ions. The structure of ALY-1 is abundant in, beta-strands and has a deep cleft, similar to the jellyroll beta-sandwich, found in 1,3-1,4-beta-glucanase. The structure suggests that alginate, molecules may penetrate into the cleft to interact with the catalytic site, of ALY-1. The reported crystal structure of another type of alginate, lyase, A1-III, differs from that of ALY-1 in that it consists almost, entirely of alpha-helical structure. Nevertheless, the putative catalytic, residues in both enzymes are positioned in space in nearly identical, arrangements. This finding suggests that both alginate lyases may have, evolved through convergent evolution.
About this StructureAbout this Structure
1UAI is a Single protein structure of sequence from Corynebacterium sp.. Active as Poly(alpha-L-guluronate) lyase, with EC number 4.2.2.11 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution., Osawa T, Matsubara Y, Muramatsu T, Kimura M, Kakuta Y, J Mol Biol. 2005 Feb 4;345(5):1111-8. Epub 2004 Dec 13. PMID:15644208
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