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OCA, Geoffrey C. Hoops

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 == General Structure and Function ==
-The EspG3 protein shown in Figure 1 has a mass of 33.7kD <ref>PMID:25275011</ref>.  The proteins beta sheets make up the backbone of the protein (yellow).  As a monomeric protein, this binds to its ligand with high specificity.  A key beta sheet region on the <scene name='69/694242/Espg3_differences/4'>β-2, β-3</scene> will vary between EspG proteins to influence what the random loop on the PE-PPE protein will interact with.  This backbone includes the key residues that interact with the random coil of the ligand.  This is surrounded by 8 alpha helices (red) which add to the structure of the protein.  One key <scene name='69/694242/Espg3_differences/2'>alpha helix</scene> will vary per EspG protein to stericly limit binding to PE-PPE ligand.  The random coil (green) connects the beta sheets and helices together, where the long <scene name='69/694242/Espg3_differences/3'>random loop</scene> variations can impact binding to the EspG's ligand.
+The EspG3 protein shown in Figure 1 has a mass of 33.7kD <ref>PMID:25275011</ref>.  The proteins beta sheets make up the core of the protein (yellow).  As a monomeric protein, this binds to its ligand with high specificity.  A key beta sheet region on the <scene name='69/694242/Espg3_differences/4'>β-2 and β-3 strands</scene> will vary between EspG subtypes to influence what the random loop on the PE-PPE protein will interact with, since this region includes key residues that interact with the random coil of the [http://proteopedia.org/wiki/index.php/PE/PPE_Protein_Complex PE-PPE] ligand.  The β-sheet core is surrounded by 8 alpha helices (red) which add to the structure of the protein.  One key <scene name='69/694242/Espg3_differences/2'>alpha helix</scene> will vary per EspG protein to stericly limit binding to PE-PPE ligand.  The random coil (green) connects the beta sheets and helices together, where the long <scene name='69/694242/Espg3_differences/3'>random loop</scene> variations can also impact binding to the EspG's ligand.
 Through specific binding factors, an EspG binds to its PE-PPE ligand to be secreted through the ESAT pathway.  Though the ESAT-6 secretion system is poorly understood, it is known that PE-PPE proteins and EspG proteins influence virulence and pathogenicity of the infection.
+==Structural Differences between EspG subtypes==
-== Structural Differences  ==
+[[Image:EspG5_and_EspG3_overlap_W.png|250 px|left|thumb|Figure 2: EspG5 (blue) and EspG3 (yellow)]]
-[[Image:EspG5_and_EspG3_overlap_W.png|250 px|left|thumb|EspG5 and EspG3]]
-Here are the key differences found on the tertiary structure of EspG3 (yellow) with EspG5(blue).  The highlighted alpha helix shows a difference in length between EspG3 and EspG5.  This difference in length contributes to the steric hinderance when binding to a PE-PPE ligand.  The random loop highlighted toward the bottom of this protein varies in length between EspG proteins, this influences binding.  The small random turn highlighted shows inconceivable difference to the EspG5 protein.  The β-2, β-3 sequence similarity between EspG5 and EspG3 is very low.
+Featured in Figure 2 are the key differences found on the tertiary structure of EspG3 (yellow) with EspG5 (blue).  The highlighted alpha helix (lower right) shows a difference in length between EspG3 and EspG5.  This difference in length contributes to the steric hinderance when binding to a PE-PPE ligand.  The random loop highlighted toward the bottom of this protein also varies in length between EspG proteins, and this influences ligand binding.  The small random turn highlighted shows inconceivable difference to the EspG5 protein.  The sequence similarity between EspG5 and EspG3 at the β-2 and β-3 strands is very low.