Crystal structure of a family 16 endoglucanase from the hyperthermophile <i>Pyrococcus furiosus</i>– structural basis of substrate recognition
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説明
<jats:p>Bacterial and archaeal endo‐β‐1,3‐glucanases that belong to glycoside hydrolase family 16 share a β‐jelly‐roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon <jats:italic>Pyrococcus furiosus</jats:italic> (<jats:italic>pf</jats:italic>LamA) has been determined at 2.1 Å resolution by molecular replacement. The <jats:italic>pf</jats:italic>LamA structure reveals a kink of six residues (72–77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic <jats:italic>Nocardiopsis </jats:italic>sp. strain F96 and <jats:italic>Bacillus macerans</jats:italic>, two proteins displaying an overall fold similar to that of <jats:italic>pf</jats:italic>LamA, but with different substrate specificity. A deletion mutant of <jats:italic>pf</jats:italic>LamA, lacking residues 72–75, hydrolyses the mixed‐linkage β‐1,3‐1,4‐glucan lichenan 10 times more efficiently than the wild‐type protein, indicating the importance of the kink in substrate preference.</jats:p>
収録刊行物
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- The FEBS Journal
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The FEBS Journal 276 (4), 1048-1058, 2009-01-23
Wiley