Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5
文献类型：期刊论文
| 作者 | Zheng, Yingying1; Huang, Chun-Hsiang1; Liu, Wenting1,2; Ko, Tzu-Ping3; Xue, Yanfen4; Zhou, Cheng4; Guo, Rey-Ting1; Ma, Yanhe1,4 |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2012-04-06 |
| 卷号 | 420期号:2页码:269-274 |
| 关键词 | Pectin Pectate lyase Trigalacturonate Ca2+ binding Crystal structure |
| 英文摘要 | The pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has great potential in industrial applications because it shows high specific activity under extremely alkaline conditions. Besides, activity measurement of Bsp165PelA does not require addition of calcium, in a way different from the other pectate lyases. Here we report crystal structures of Bsp165PelA in apo-form and in complex with trigalacturonate. The parallel beta-helix, active site residues and substrate binding cleft are similar to those in the other pectate lyases from Polysaccharide Lyase family 1. However, some of the highly conserved Ca2+ binding residues and secondary structures are altered in Bsp165PelA, making it difficult to coordinate with Ca2+ as in the other pectate lyases. We found Bsp165PelA forms some direct enzyme-substrate interactions instead of using Ca2+ ions bridging in the extremely alkaline environment. (C) 2012 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | REFINED 3-DIMENSIONAL STRUCTURE ; ERWINIA-CHRYSANTHEMI ; SEQUENCE ALIGNMENT ; SOFTWARE ; PROTEINS ; RESOLUTION ; MECHANISM ; TOOLS ; FOLDS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000306042100010 |
| 源URL | [http://124.16.173.210/handle/834782/1314]  |
| 专题 | 天津工业生物技术研究所_结构生物学与蛋白酶学实验室 郭瑞庭_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Ind Enzymes Natl Engn Lab, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China 2.Tianjin Univ Sci & Technol, Tianjin 300457, Peoples R China 3.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan 4.Chinese Acad Sci, State Key Lab Microbial Resources, Inst Microbiol, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zheng, Yingying,Huang, Chun-Hsiang,Liu, Wenting,et al. Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2012,420(2):269-274. |
| APA | Zheng, Yingying.,Huang, Chun-Hsiang.,Liu, Wenting.,Ko, Tzu-Ping.,Xue, Yanfen.,...&Ma, Yanhe.(2012).Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,420(2),269-274. |
| MLA | Zheng, Yingying,et al."Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 420.2(2012):269-274. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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