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dc.contributor.author | Mikami, Bunzo | en |
dc.contributor.author | Ban, Mizuho | en |
dc.contributor.author | Suzuki, Sachiko | en |
dc.contributor.author | Yoon, Hye-Jin | en |
dc.contributor.author | Miyake, Osamu | en |
dc.contributor.author | Yamasaki, Masayuki | en |
dc.contributor.author | Ogura, Kohei | en |
dc.contributor.author | Maruyama, Yukie | en |
dc.contributor.author | Hashimoto, Wataru | en |
dc.contributor.author | Murata, Kousaku | en |
dc.contributor.alternative | 三上, 文三 | ja |
dc.date.accessioned | 2012-11-08T06:09:51Z | - |
dc.date.available | 2012-11-08T06:09:51Z | - |
dc.date.issued | 2012-09 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.uri | http://hdl.handle.net/2433/161048 | - |
dc.description.abstract | 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. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | International Union of Crystallography | en |
dc.rights | © 2012 International Union of Crystallography Printed in Singapore | en |
dc.subject | alginate lyase | en |
dc.subject | loop hinge motion | en |
dc.subject | catalytic mechanism | en |
dc.subject | flexible loop | en |
dc.title | Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA10885500 | - |
dc.identifier.jtitle | Acta crystallographica. Section D, Biological crystallography | en |
dc.identifier.volume | 68 | - |
dc.identifier.issue | Part 9 | - |
dc.identifier.spage | 1207 | - |
dc.identifier.epage | 1216 | - |
dc.relation.doi | 10.1107/S090744491202495X | - |
dc.textversion | publisher | - |
dc.identifier.pmid | 22948922 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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