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==Binding Specificity of EspG Proteins to PE-PPE Proteins in ''mycobacterium tuberculosis''==
==Binding Specificity of EspG Proteins to PE-PPE Proteins in ''mycobacterium tuberculosis''==
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<StructureSection load='4KXR' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='4KXR' size='340' side='right' caption='Here shows PE25-PPE41 lignad bound to EspG5 protein. Resolution 2.60Å' scene=''>
EspG secretion is key in understanding the virulence of ''mycobacterium tuberculosis''. The specificity of EspG binding affinity to its specific PE-PPE ligand have many contributing factors. The four different EspG proteins found in ''mycobacterium tuberculosis'' have different characteristics that influence binding, where EspG5 binds to the most PE-PPE proteins. Here EspG5 binds to PE25-PPE41 to be excreted in the ESAT-6 pathway.
EspG secretion is key in understanding the virulence of ''mycobacterium tuberculosis''. The specificity of EspG binding affinity to its specific PE-PPE ligand have many contributing factors. The four different EspG proteins found in ''mycobacterium tuberculosis'' have different characteristics that influence binding, where EspG5 binds to the most PE-PPE proteins. Here EspG5 binds to PE25-PPE41 to be excreted in the ESAT-6 pathway.

Revision as of 12:12, 31 March 2015

Binding Specificity of EspG Proteins to PE-PPE Proteins in mycobacterium tuberculosis

Here shows PE25-PPE41 lignad bound to EspG5 protein. Resolution 2.60Å

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References

  1. Ekiert DC, Cox JS. Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion. Proc Natl Acad Sci U S A. 2014 Oct 14;111(41):14758-63. doi:, 10.1073/pnas.1409345111. Epub 2014 Oct 1. PMID:25275011 doi:http://dx.doi.org/10.1073/pnas.1409345111
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