Sandbox Reserved 1075

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==Binding Specificity of EspG Proteins to PE-PPE Proteins in ''mycobacterium tuberculosis''==
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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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<StructureSection load='4W4I' size='340' side='right' caption='Caption for this structure' scene=''>
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==Your Protein Name here==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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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.
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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[[Image:EspG3.png|300 px|right|thumb|Figure Legend]]
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== Biological Function ==
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== Function ==
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== Structural Overview ==
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a;lksdja;lskdjfa;lsdkfjas;ldkfja;sldkfj
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=== Excretion ===
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== Mechanism of Action ==
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EspG PE-PPE excretion is done through the ESX secretion pathway.
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=== Binding ===
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== Zinc Ligand(s) ==
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Factors that influence binding of EspG and PE-PPE:
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electrostatics
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shape
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ligand random coil
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key catalytic residues
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=== Pocket Residues ===
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== Other Ligands ==
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Jon
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== Structural highlights ==
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== Relevance ==
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== Publication Abstract from PubMed ==
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Nearly 10% of the coding capacity of the Mycobacterium tuberculosis genome is devoted to two highly expanded and enigmatic protein families called PE and PPE, some of which are important virulence/immunogenicity factors and are secreted during infection via a unique alternative secretory system termed "type VII." How PE-PPE proteins function during infection and how they are translocated to the bacterial surface through the five distinct type VII secretion systems [ESAT-6 secretion system (ESX)] of M. tuberculosis is poorly understood. Here, we report the crystal structure of a PE-PPE heterodimer bound to ESX secretion-associated protein G (EspG), which adopts a novel fold. This PE-PPE-EspG complex, along with structures of two additional EspGs, suggests that EspG acts as an adaptor that recognizes specific PE-PPE protein complexes via extensive interactions with PPE domains, and delivers them to ESX machinery for secretion. Surprisingly, secretion of most PE-PPE proteins in M. tuberculosis is likely mediated by EspG from the ESX-5 system, underscoring the importance of ESX-5 in mycobacterial pathogenesis. Moreover, our results indicate that PE-PPE domains function as cis-acting targeting sequences that are read out by EspGs, revealing the molecular specificity for secretion through distinct ESX pathways.
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Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion.,Ekiert DC, Cox JS 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<ref>PMID:25275011</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
</StructureSection>
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<scene name='69/697501/Helix_highlited/1'>Helix Highlited</scene>
 
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
== References ==
== References ==
<references/>
<references/>

Current revision

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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