1.37 Å Crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli

被引：2
|
作者：
Tang, Qun [1 ,2 ]
Liu, Yan-Ping [2 ]
Ren, Zheng-Guang [1 ]
Yan, Xiao-Xue [2 ]
Zhang, Li-Qun [1 ]
机构：
[1] China Agr Univ, Dept Plant Pathol, Beijing 100193, Peoples R China
[2] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2013年 / 81卷 / 08期
基金：
中国国家自然科学基金;
关键词：
pectate lyase; pathogenic factor; Acidovorax citrulli; crystal structure; right-handed; -helix; SEQUENCE ALIGNMENT; BINDING;
D O I：
10.1002/prot.24298
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：
Pectates lyase (Pel) plays an important role in bacteria pathogenicity. The crystal structure of Pel from Acidovorax citrulli (AcPel) has been solved to 1.37 angstrom resolution. AcPel belongs to the polysaccharide lyase family 1 (PL1), which has a characteristic right-handed -helix fold. AcPel is similar with other Pels in the PL1 family, but also shows some differences at the substrate binding site. Proteins 2013; 81:1485-1490. (c) 2013 Wiley Periodicals, Inc.
引用
收藏
页码：1485 / 1490
页数：6
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