Sandbox Reserved 386: Difference between revisions

MtrF contains a few common <scene name='Sandbox_Reserved_386/Elements/2'>elements</scene>; O,N,Fe and Ca. Oxygen is the most abundant element and is spread out through the entire protein, there are several Nitrogens that form rings that have an Iron placed in the center, there is also a lone Calcium ion. There are <scene name='Sandbox_Reserved_386/Alpha_beta/1'>alpha helices and beta sheets</scene> positioned throughout MtrF, there are more alpha helices but they are randomly placed in the structure while there are fewer beta sheets and they are located on opposite ends from one another. MtrF as mentioned above is a decaheme cytochrome, which means that there are ten heme groups that are spatially organized throughout the protein. Each heme is spread about 7Å from its neighbor, this close space allows for speedy electron transfer. The (ten) hemes are organized across four domains in a distinctive cross conformation, a staggered 65-? Octaheme chain intersects the protein and is bisected by a planar 45-? Tetraheme chain. All of the hemes in the MtrF crystal structure display bis-His axial ligand coordination. The His residue in the domains provide the distal ligands for the five hemes in the same domain. Domains I and III contain antiparallel Beta-strands that connect two Greek key split Beta-barrel domains. Domains II and IV bind five closely packed hemes covalently attached Cys residues to the motifs in each domain. All the domains fold together so that the pentaheme domains II and IV are crowded together to form a central core with the two barrel domains I and III adjoining either side. The 3.2Å crystal structure proposes that the hemes, each corresponding to two His ligands, are near enough for effective electron transfer. Near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy provide additional support for these structural features. The complete structure of MtrF is similar to an ellipsoid with dimensions of 85x70x30Å. This particular structure was able to provide molecular insight into how the reduction of insoluble substrates, soluble substrates, and cytochrome redox partners may be possible together at different termini on an electron transport chain on the cell surface.<ref name="mtrf" />

''Neisseria gonorrhoeae'' is the bacteria that causes the STD Gonorrhea. This bacteria is quite resistant to many hydrophobic drugs, detergents, and dyes. The reason behind the tough resistance is the energy dependent efflux pump Mtr(Multiple transferable resistance).  MtrF has been identified as a cell envelope protein that is involved with the resistance of hydrophobic antimicrobials in ''Neisseria gonorrhoeae''. MtrF is a protein that helps highlight the expression of detergent resistance by gonococci. MtrF is thought to act in accordance with the MtrC- MtrD- MtrE efflux pump; to make sure gonococci has high level resistance to specific hydrophobic agents. MtrF is located near the MtrR gene and is predicted to encode a cytoplasmic membrane protein that contains up to twelve transmembrane domains. The expression of MtrF is ultimately subject to MtrR’s transcriptional control. MtrF was given its name because it’s so closely tied to the protein MtrR. Several orthologues were discovered in a few Gram-negative and positive bacteria, indicating that perhaps the predicted products may represent an undescribed protein family that is highly involved with resistance of antimicrobials. <ref> PMID:12493784 </ref>