Exotoxin: Difference between revisions

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<StructureSection load='3q9o' size='340' side='right' caption='Structure of Vibrio cholerae exotoxin complex with NAD and glycerol (PDB code [[3q9o]]).' scene=''>
<StructureSection load='3q9o' size='400' side='right' caption='Structure of Vibrio cholerae exotoxin complex with NAD and glycerol (PDB code [[3q9o]]).' scene='59/593276/Cv/1'>
 
== Function ==
== Function ==


Exotoxins (ET) are toxins which are secreted by bacteria.
Exotoxins (ET) are toxins which are secreted by Gram-positive and Gram-negative bacteria<ref>PMID:17675409</ref>. ETs are heat labile.  They are highly toxic and fatal in μg quantities.  ETs bind to specific receptors and have no enzymatic activity.


== Disease ==
== Relevance ==


== Relevance ==
Exotoxins are involved in tetanus, diphtheria and botulism.


== Structural highlights ==
== Structural highlights ==
</StructureSection>
 
<scene name='59/593276/Cv/4'>NAD binding site</scene> in ''Vibrio cholerae'' exotoxin (PDB code [[3q9o]]).<ref>PMID:22535961</ref> Water molecules shown as red spheres.


==3D structures of exotoxin==
==3D structures of exotoxin==
[[Exotoxin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*''Pseudomonas aeruginosa'' exotoxin
 
**[[1ikq]] – PaET A <br />
**[[1ikp]] – PaET A (mutant) <br />
**[[1dma]] – PaET A catalytic domain + nicotinamide + AMP <br />
**[[1aer]] – PaET A catalytic domain + NAD analog + AMP <br />
**[[1xk9]] – PaET A catalytic domain + inhibitor <br />
**[[1zm2]] – PaET A catalytic domain + diphthamide + adenosine diphosphoribose + EF-2 <br />
**[[1zm3]] – PaET A catalytic domain + diphthamide + EF-2 <br />
**[[3b78]], [[2zit]] – PaET A catalytic domain + diphthamide + NAD + EF-2 <br />
**[[3b82]], [[3b8h]] – PaET A catalytic domain (mutant) + diphthamide + NAD + EF-2 <br />
**[[1zm4]] – PaET A catalytic domain + diphthamide + NAD analog + EF-2 <br />
**[[1zm9]] – PaET A catalytic domain + diphthamide + inhibitor + EF-2 <br />
 
*''Vibrio cholerae'' exotoxin
 
**[[2q5t]] – VcET <br />
**[[2q6m]], [[3ess]], [[3ki0]], [[3ki1]], [[3ki2]], [[3ki3]], [[3ki4]], [[3ki5]], [[3ki6]], [[3ki7]], [[3ny6]] – VcET catalytic domain + inhibitor <br />
**[[3q9o]] – VcET + NAD <br />
 
*''Streptococcus pyogenes'' exotoxin
 
**[[1b1z]], [[1fnu]], [[1fnv]], [[1fnw]] – SpET A1 <br />
**[[1dki]] – SpET B<br />
**[[2jtc]] – SpET B (mutant) - NMR<br />
**[[1an8]] – SpET C<br />
**[[1et9]] – SpET H<br />
**[[1ty0]] – SpET J<br />
**[[1ha5]], [[1uup]] – SpET A1 + Zn<br />
**[[1l0x]] – SpET A1 (mutant) + T cell receptor β chain<br />
**[[1pvj]] – SpET B + inhibitor <br />
**[[2uzj]] – SpET B + guanidine derivative <br />
**[[1eu4]] – SpET H + Zn<br />
**[[1ty2]] – SpET J + Zn<br />
**[[1ktk]] – SpET C (mutant) + T cell receptor β chain<br />
**[[1l0y]] – SpET A1 (mutant) + T cell receptor β chain + Zn<br />
**[[1hqr]] – SpRT C + antibody + myelin basic protein<br />
 
*''Staphylococcus aureus'' exotoxin
 
**[[1v1o]], [[1v1p]] – SaET 1 <br />
**[[2r61]], [[2z8l]] – SaET 3<br />
**[[3o13]] – SaET 15<br />
**[[3kls]] – SaET 1 (mutant) + complement C5<br />
 
*''Corynebacterium diphtheriae'' exotoxin See [[Diphtheria toxin]]
 
}}
 
 
 


== References ==
== References ==

Latest revision as of 12:16, 25 June 2019

Function

Exotoxins (ET) are toxins which are secreted by Gram-positive and Gram-negative bacteria[1]. ETs are heat labile. They are highly toxic and fatal in μg quantities. ETs bind to specific receptors and have no enzymatic activity.

Relevance

Exotoxins are involved in tetanus, diphtheria and botulism.

Structural highlights

in Vibrio cholerae exotoxin (PDB code 3q9o).[2] Water molecules shown as red spheres.

3D structures of exotoxin

Exotoxin 3D structures


Structure of Vibrio cholerae exotoxin complex with NAD and glycerol (PDB code 3q9o).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Hamon MA, Batsche E, Regnault B, Tham TN, Seveau S, Muchardt C, Cossart P. Histone modifications induced by a family of bacterial toxins. Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13467-72. Epub 2007 Aug 3. PMID:17675409 doi:http://dx.doi.org/10.1073/pnas.0702729104
  2. ↑ Fieldhouse RJ, Jorgensen R, Lugo MR, Merrill AR. The 1.8 angstrom cholix toxin crystal structure in complex with NAD and evidence for a new kinetic model. J Biol Chem. 2012 Apr 25. PMID:22535961 doi:10.1074/jbc.M111.337311

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Michal Harel, Alexander Berchansky
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