TY - JOUR
T1 - Crystal structure of the alginate (Poly α-L-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution
AU - Osawa, Takuo
AU - Matsubara, Yasuhito
AU - Muramatsu, Tsuyoshi
AU - Kimura, Makoto
AU - Kakuta, Yoshimitsu
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2005/2/4
Y1 - 2005/2/4
N2 - The crystal structure of alginate (poly α-l-guluronate) lyase from Corynebacterium sp. (ALY-1) was determined at 1.2 Å resolution using the MAD method and bromide ions. The structure of ALY-1 is abundant in β-strands and has a deep cleft, similar to the jellyroll β-sandwich found in 1,3-1,4-β-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 α-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.
AB - The crystal structure of alginate (poly α-l-guluronate) lyase from Corynebacterium sp. (ALY-1) was determined at 1.2 Å resolution using the MAD method and bromide ions. The structure of ALY-1 is abundant in β-strands and has a deep cleft, similar to the jellyroll β-sandwich found in 1,3-1,4-β-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 α-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.
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U2 - 10.1016/j.jmb.2004.10.081
DO - 10.1016/j.jmb.2004.10.081
M3 - Article
C2 - 15644208
AN - SCOPUS:11844301646
SN - 0022-2836
VL - 345
SP - 1111
EP - 1118
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 5
ER -