Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp N16-5

被引：34
|
作者：
Zheng, Yingying [1 ]
Huang, Chun-Hsiang [1 ]
Liu, Wenting [1 ,2 ]
Ko, Tzu-Ping [3 ]
Xue, Yanfen [4 ]
Zhou, Cheng [4 ]
Guo, Rey-Ting [1 ]
Ma, Yanhe [1 ,4 ]
机构：
[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
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 420卷 / 02期
关键词：
Pectin; Pectate lyase; Trigalacturonate; Ca2+ binding; Crystal structure; REFINED 3-DIMENSIONAL STRUCTURE; ERWINIA-CHRYSANTHEMI; SEQUENCE ALIGNMENT; SOFTWARE; PROTEINS; RESOLUTION; MECHANISM; TOOLS; FOLDS;
D O I：
10.1016/j.bbrc.2012.02.148
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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.
引用
收藏
页码：269 / 274
页数：6
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