Crystal structure of the alginate (Poly α-L-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution

Takuo Osawa, Yasuhito Matsubara, Tsuyoshi Muramatsu, Makoto Kimura, Yoshimitsu Kakuta

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1111-1118
Number of pages8
JournalJournal of Molecular Biology
Volume345
Issue number5
DOIs
Publication statusPublished - Feb 4 2005

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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