The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens: expression, purification and crystallographic analysis

被引:2
|
作者
Churchill-Angus, Alicia M. [1 ]
Sedelnikova, Svetlana E. [1 ]
Schofield, Thomas H. B. [1 ,2 ]
Baker, Patrick J. [1 ]
机构
[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Western Bank, Sheffield S10 2TN, S Yorkshire, England
[2] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2020年 / 76卷
基金
英国工程与自然科学研究理事会;
关键词
pore-forming toxin; crystallization; ClyA family; Serratia; RAY CRYSTAL-STRUCTURE; BACILLUS-CEREUS NHE; HEMOLYSIN-BL; COMPLEX; SHEA; CLYA;
D O I
10.1107/S2053230X20013862
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Tripartite alpha-pore-forming toxins are constructed of three proteins (A, B and C) and are found in many bacterial pathogens. While structures of the B and C components from Gram-negative bacteria have been described, the structure of the A component of a Gram-negative alpha-pore-forming toxin has so far proved elusive. SmhA, the A component from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein and anomalous data were collected. Phases were calculated and an initial electron-density map was produced.
引用
收藏
页码:577 / 582
页数:6
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