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タイトル: | Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III. |
著者: | Mikami, Bunzo ![]() ![]() Ban, Mizuho Suzuki, Sachiko Yoon, Hye-Jin Miyake, Osamu Yamasaki, Masayuki ![]() Ogura, Kohei Maruyama, Yukie Hashimoto, Wataru ![]() ![]() ![]() Murata, Kousaku |
著者名の別形: | 三上, 文三 |
キーワード: | alginate lyase loop hinge motion catalytic mechanism flexible loop |
発行日: | Sep-2012 |
出版者: | International Union of Crystallography |
誌名: | Acta crystallographica. Section D, Biological crystallography |
巻: | 68 |
号: | Part 9 |
開始ページ: | 1207 |
終了ページ: | 1216 |
抄録: | The structures of two mutants (H192A and Y246F) of a mannuronate-specific alginate lyase, A1-III, from Sphingomonas species A1 complexed with a tetrasaccharide substrate [4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)(2)-mannuronic acid] were determined by X-ray crystallography at around 2.2 Å resolution together with the apo form of the H192A mutant. The final models of the complex forms, which comprised two monomers (of 353 amino-acid residues each), 268-287 water molecules and two tetrasaccharide substrates, had R factors of around 0.17. A large conformational change occurred in the position of the lid loop (residues 64-85) in holo H192A and Y246F compared with that in apo H192A. The lid loop migrated about 14 Å from an open form to a closed form to interact with the bound tetrasaccharide and a catalytic residue. The tetrasaccharide was bound in the active cleft at subsites -3 to +1 as a substrate form in which the glycosidic linkage to be cleaved existed between subsites -1 and +1. In particular, the O(η) atom of Tyr68 in the closed lid loop forms a hydrogen bond to the side chain of a presumed catalytic residue, O(η) of Tyr246, which acts both as an acid and a base catalyst in a syn mechanism. |
著作権等: | © 2012 International Union of Crystallography Printed in Singapore |
URI: | http://hdl.handle.net/2433/161048 |
DOI(出版社版): | 10.1107/S090744491202495X |
PubMed ID: | 22948922 |
出現コレクション: | 学術雑誌掲載論文等 |
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