Crystal structure of the Legionella effector Lem22

被引：3

作者：

Kozlov, Guennadi ^{[1
]}

Wong, Kathy ^{[1
]}

Gehring, Kalle ^{[1
]}

机构：

[1] McGill Univ, Dept Biochem, Grp Rech Struct Prot, 3649 Promenade Sir William Osler, Montreal, PQ H3G 0B1, Canada

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2018年 / 86卷 / 02期

基金：

美国国家卫生研究院; 加拿大健康研究院; 美国国家科学基金会;

关键词：

Legionella; lpg2328; pathogen; virulence factor; X-ray crystallography; PROTEINS; REFINEMENT;

D O I：

10.1002/prot.25427

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：

Legionella pneumophila is a pathogen causing severe pneumonia in humans called Legionnaires' disease. Lem22 is a previously uncharacterized effector protein conserved in multiple Legionella strains. Here, we report the crystal structure of Lem22 from the Philadelphia strain, also known as lpg2328, at 1.40 angstrom resolution. The structure shows an up-and-down three-helical bundle with a significant structural similarity to a number of protein-binding domains involved in apoptosis and membrane trafficking. Sequence conservation identifies a putative functional site on the interface of helices 2 and 3. The structure is an important step toward a functional characterization of Lem22.

引用

页码：263 / 267

页数：5

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