Exotoxin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<scene name='59/593276/Cv/ | <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. | ||
</StructureSection> | </StructureSection> |
Revision as of 14:13, 14 March 2019
FunctionExotoxins (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. RelevanceExotoxins are involved in tetanus, diphtheria and botulism. Structural highlightsin Vibrio cholerae exotoxin (PDB code 3q9o).[2] Water molecules shown as red spheres.
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3D structures of exotoxin3D structures of exotoxin
Updated on 14-March-2019
ReferencesReferences
- ↑ 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
- ↑ 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