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 journalArticle

48 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

Fingerprint

Corynebacterium
Lyases
Bromides
Catalytic Domain
Ions
Enzymes
poly(beta-D-mannuronate) lyase
alginic acid
mycophenolic adenine dinucleotide

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

Crystal structure of the alginate (Poly α-L-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution. / Osawa, Takuo; Matsubara, Yasuhito; Muramatsu, Tsuyoshi; Kimura, Makoto; Kakuta, Yoshimitsu.

In: Journal of Molecular Biology, Vol. 345, No. 5, 04.02.2005, p. 1111-1118.

Research output: Contribution to journalArticle

Osawa, Takuo ; Matsubara, Yasuhito ; Muramatsu, Tsuyoshi ; Kimura, Makoto ; Kakuta, Yoshimitsu. / Crystal structure of the alginate (Poly α-L-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution. In: Journal of Molecular Biology. 2005 ; Vol. 345, No. 5. pp. 1111-1118.
@article{136777c3bb9043c9b70e95ead021b75f,
title = "Crystal structure of the alginate (Poly α-L-guluronate) lyase from Corynebacterium sp. at 1.2 {\AA} resolution",
abstract = "The crystal structure of alginate (poly α-l-guluronate) lyase from Corynebacterium sp. (ALY-1) was determined at 1.2 {\AA} 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.",
author = "Takuo Osawa and Yasuhito Matsubara and Tsuyoshi Muramatsu and Makoto Kimura and Yoshimitsu Kakuta",
year = "2005",
month = "2",
day = "4",
doi = "10.1016/j.jmb.2004.10.081",
language = "English",
volume = "345",
pages = "1111--1118",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "5",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=11844301646&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=11844301646&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2004.10.081

DO - 10.1016/j.jmb.2004.10.081

M3 - Article

VL - 345

SP - 1111

EP - 1118

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 5

ER -