Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus

详细信息	查看全文 | 推荐本文 |

• 作者：Han-Woo Kim ; Misumi Kataoka ; Kazuhiko Ishikawa ; ^{kazu-ishikawa@aist.go.jp}
• 关键词：Hyperthermophile ; Endocellulase ; Archaea ; Crystal structure ; DxDxDG calcium-binding motif ; Pyrococcus furiosus
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：5 April, 2012
• 卷：586
• 期：7
• 页码：1009-1013
• 文件大小：1172 K

摘要

Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of 尾-1,4-glucosidic linkage in 尾-glucan cellulose. A truncated EGPf (EGPf螖N30) mutant lacking the proline and hydroxyl-residue rich region at the N terminus was constructed, and its crystal structure was resolved at an atomic resolution of 1.07 脜. Our results indicate that the structure of EGPf, which consists of a 尾-jelly roll, exhibits structural similarity with the endocellulase of Thermotoga maritima. Additionally, we further determined that the thermostability of EGPf is maintained in part by the binding of in a DxDxDG -binding motif, atypical of most archaeal proteins.