Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 345, Issue 5, Pages 1111-1118Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2004.10.081
Keywords
crystal structure; alginate lyase; poly(alpha-L-guluronate) lyase; Corynebacterium sp.; convergent evolution
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The crystal structure of alginate (poly alpha-L-guluronate). lyase from Corynebacterium sp. (ALY-1) was determined at 1.2 Angstrom 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. (C) 2004 Elsevier Ltd. All rights reserved.
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