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==MgtC: A Virulence Factor From ''Mycobacterium tuberculosis''== | ==MgtC: A Virulence Factor From ''Mycobacterium tuberculosis''== | ||
<StructureSection load='2lqj' size='350' side='right' caption='MgtC Protein' scene=''> | <StructureSection load='2lqj' size='350' side='right' caption='MgtC Protein' scene='69/698113/Rainbow-colored_spectrum/1'>TextToBeDisplayed'> | ||
The MgtC protein is a membrane-bound protein that has been found to be a critical virulence factor for intramacrophage growth. | The MgtC protein is a membrane-bound protein that has been found to be a critical virulence factor for intramacrophage growth. | ||
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== Function == | == Function == | ||
This domain of MgtC, in contrast, is highly variable in comparison to several orthologues, as presented by Yang et al. However, through a sequence alignment of five known functional MgtC orthologues from pathogens that survive inside macrophages (''M. tuberculosis, B. melitensis, B. cenocepacia, Y. pestis,'' and ''S. Typhimurium''), seven strictly conserved residues were found to be scattered along the whole sequence of the relatively hydrophilic and soluble C-terminal domain. | |||
A large hydrophobic core has conserved residues <scene name='69/698113/Conserved_core_residues/3'>Cysteine-155, Arginine-164, Glutamine-160, and Alanine-195</scene>. | |||
[[Image:Final_Final_Core_Logo.PNG |625× 116px|thumb|left|Four strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain.]] | |||
The opposite side of the protein has a small cluster of conserved residues <scene name='69/698113/Conserved_surface_residues/1'>Tyrosine-149, Glutamine-208, and Tryptophan-225</scene>. | |||
[[Image:Final_Surface_Web_Logo.PNG |625× 121px|thumb|left|Four strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain.]] | |||
[[Image:Entire_Web_Logo.PNG |617 × 125 px|thumb|left|Seven strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain.]] | |||
In the | |||
Additionally, there is a crystal structure available for this domain. When comparing the crystal structure of the C-terminal domain to other protein structures, there are striking similarities between this domain and a class of proteins known as ACT domains. | |||
===Mechanism=== | ===Mechanism=== | ||
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[[Image:2lqj_colorful.png |100 px|left|thumb|Simple Structure]] | [[Image:2lqj_colorful.png |100 px|left|thumb|Simple Structure]] | ||
Among the family of MgtC proteins, there are very few residues that are conserved, especially among a highly variable C-terminal. Three conserved residues exist on the <scene name='69/698113/Conserved_surface/1'>surface</scene> of the protein. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 22:39, 17 April 2015
MgtC: A Virulence Factor From Mycobacterium tuberculosisMgtC: A Virulence Factor From Mycobacterium tuberculosis
TextToBeDisplayed'> The MgtC protein is a membrane-bound protein that has been found to be a critical virulence factor for intramacrophage growth. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. FunctionThis domain of MgtC, in contrast, is highly variable in comparison to several orthologues, as presented by Yang et al. However, through a sequence alignment of five known functional MgtC orthologues from pathogens that survive inside macrophages (M. tuberculosis, B. melitensis, B. cenocepacia, Y. pestis, and S. Typhimurium), seven strictly conserved residues were found to be scattered along the whole sequence of the relatively hydrophilic and soluble C-terminal domain. A large hydrophobic core has conserved residues .  The opposite side of the protein has a small cluster of conserved residues . 
 In the Additionally, there is a crystal structure available for this domain. When comparing the crystal structure of the C-terminal domain to other protein structures, there are striking similarities between this domain and a class of proteins known as ACT domains.
MechanismStructural highlights Among the family of MgtC proteins, there are very few residues that are conserved, especially among a highly variable C-terminal. Three conserved residues exist on the of the protein.
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ReferencesReferences
- ↑ 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
- ↑ 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