Crystal Structure of the Alginate (Poly α-l-guluronate) Lyase from Corynebacterium sp. at 1.2Å Resolution

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-...

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Bibliographic Details
Published in:Journal of molecular biology 2005-04, Vol.345 (5), p.1111-1118
Main Authors: Osawa, T, Matsubara, Y, Muramatsu, T, Kimura, M, Kakuta, Y
Format: Article
Language:English
Subjects:
Corynebacterium
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Summary: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.
ISSN:0022-2836
DOI:10.1016/j.jmb.2004.10.081