Anthrax protective antigen: Difference between revisions
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<StructureSection load='1acc' size=' | <StructureSection load='1acc' size='350' side='right' caption='Anthrax protective antigen (PA83) complex with Ca+2 ions (PDB code [[1acc]])' scene='48/485625/Cv/8'> | ||
__TOC__ | |||
== Function == | |||
'''Anthrax protective antigen''' (PA) is the cell-binding part of the ''Bacillus anthracis'' anthrax toxin. The anthrax toxin is composed of the PA, lethal factor and edema factor. The PA translocates the [[Anthrax Lethal Factor|lethal]] (LF) and [[Anthrax edema factor|edema]] factors (EF) into the cell. The 83kD form of PA '''(PA83)''' binds to the anthrax toxin receptor. A 20kD fragment (PA20) is cleaved off the PA83 and the remaining '''PA63''' assembles into ring-shaped oligomer which becomes a membrane pre-channel. The PA pre-channel binds the lethal and edema factors allowing them to penetrate the membrane via pH gradient. | |||
For more details see | |||
*[[Molecular Playground/Protective Antigen]]<br /> | |||
*[[Anthrax Toxin Protein]]<br /> | |||
*[[Toxins]]. | |||
== Structural highlights == | == Structural highlights == | ||
PA contains 4 domains:<br /> | PA contains 4 domains:<br /> | ||
* Domain 1 is the N terminal. It contains the furin protease cleavage site enabling the release of PA20.<br /> | * <scene name='48/485625/Cv/3'>Domain 1</scene> is the N terminal (in yellow). It contains the furin protease cleavage site enabling the release of PA20.<br /> | ||
* Domain 2 is the heptamerization domain of PA63.<br /> | * <scene name='48/485625/Cv/4'>Domain 2</scene> (in cyan) is the heptamerization domain of PA63.<br /> | ||
* Domain 3 forms the heptameric pore with domain 2 and enabling LF and EF to penetrate the cell.<br /> | * <scene name='48/485625/Cv/5'>Domain 3</scene> (in salmon) forms the heptameric pore with domain 2 and enabling LF and EF to penetrate the cell.<br /> | ||
* Domain 4 is important for receptor recognition and pore formation. <br /> | * <scene name='48/485625/Cv/6'>Domain 4</scene> (in magenta) is important for receptor recognition and pore formation. <br /> | ||
<scene name='48/485625/Cv/11'>Click here to see Ca binding site</scene>. <ref>PMID:9039918</ref> | |||
</ | |||
==3D structures of anthrax protective antigen== | ==3D structures of anthrax protective antigen== | ||
[[Anthrax protective antigen 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Latest revision as of 13:09, 26 May 2024
FunctionAnthrax protective antigen (PA) is the cell-binding part of the Bacillus anthracis anthrax toxin. The anthrax toxin is composed of the PA, lethal factor and edema factor. The PA translocates the lethal (LF) and edema factors (EF) into the cell. The 83kD form of PA (PA83) binds to the anthrax toxin receptor. A 20kD fragment (PA20) is cleaved off the PA83 and the remaining PA63 assembles into ring-shaped oligomer which becomes a membrane pre-channel. The PA pre-channel binds the lethal and edema factors allowing them to penetrate the membrane via pH gradient. For more details see Structural highlightsPA contains 4 domains:
. [1] 3D structures of anthrax protective antigenAnthrax protective antigen 3D structures
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ReferencesReferences
- ↑ Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC. Crystal structure of the anthrax toxin protective antigen. Nature. 1997 Feb 27;385(6619):833-8. PMID:9039918 doi:10.1038/385833a0