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The CusC protein does not have any obvious features that would make it specific for metal ions, suggesting that the narrow substrate specificity of the pump is provided by other components of the pump, most likely by the inner membrane component CusA.
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In conclusion, CusC does not show structural features that would confer specificity towards metal ions, confirming phylogenetic analyses [4] and indicating that the narrow substrate specificity of the Cus pump most likely is caused by the inner membrane RND component CusA.
The wide substrate specificity of these pumps could allow them to provoke extrusion of various active antibacterial compounds, preventing their inhibitory effects [ 9].
The wide substrate specificity of these pumps, as well as their widespread among bacterial species make us believe that these efflux pumps are also responsible for the extrusion of various active compounds from the plant extract out of bacteria cells, therefore preventing their inhibitory effects.
This type of interaction may allow a wider range of peptides to be pumped into the ER and in turn be presented by class I. Second, the TAP genes may interact in a specific manner, and may pump peptides for binding to specific class I genes or only in certain tissues, increasing the specificity of peptides pumped into the ER.
We have compared the CusC structure with the structures of other OMF proteins to obtain insight in whether CusC is likely to contribute to the observed substrate specificity of the Cus metal efflux pump.
The structural determinants for the broad substrate specificity of Pdrp pumps have not yet been identified even though dozens of publications have reported hundreds of amphiphilic substrates for Pdr5p and Snq2p.
The specificity of P-type pumps was inferred by phylogenetic analysis of all of the P-type cation transporters found from A. pullulans and their homologues with known function from other fungi, as described in [ 54].
These transporters differ in the source of energy used to pump out the drug and in the specificity of the azole molecule.
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However, regenerating the surfaces of the pump channels daily will limit the pump's applications.
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