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

Autor:	Patrick J. Baker, Svetlana E. Sedelnikova, Thomas H. B. Schofield, Alicia M. Churchill-Angus
Rok vydání:	2020
Předmět:	Serratia crystallization Bacterial Toxins Biophysics Human pathogen Crystallography X-Ray medicine.disease_cause Biochemistry Research Communications 03 medical and health sciences 0302 clinical medicine Structural Biology Genetics medicine pore-forming toxin Cloning Molecular Serratia marcescens 030304 developmental biology 0303 health sciences Pore-forming toxin biology Chemistry Component (thermodynamics) Toxin Condensed Matter Physics biology.organism_classification ClyA family 030217 neurology & neurosurgery Bacteria
Zdroj:	Acta Crystallographica. Section F, Structural Biology Communications
ISSN:	2053-230X
DOI:	10.1107/s2053230x20013862
Popis:	SmhA, the A component of the tripartite α-pore-forming toxin from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein, anomalous data were collected, phases were calculated and an initial electron-density map was produced. 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.
Databáze:	OpenAIRE
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