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The A component (SmhA) of a tripartite pore‐forming toxin from Serratia marcescens : expression, purification and crystallographic analysis
Author(s) -
Churchill-Angus Alicia M.,
Sedelnikova Svetlana E.,
Schofield Thomas H. B.,
Baker Patrick J.
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20013862
Subject(s) - serratia marcescens , serratia , toxin , pore forming toxin , pathogen , microbiology and biotechnology , bacteria , gram , chemistry , component (thermodynamics) , biology , escherichia coli , microbial toxins , biochemistry , physics , genetics , pseudomonas , gene , thermodynamics
Tripartite α‐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 α‐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.