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

页码：577 / 582

页数：6

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