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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.

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 .

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 .

Four strictly conserved residues of five known functional MgtC orthologs of the soluble C-terminal domain.

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

Structural highlights

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 of the protein.