TolA: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Laura McCauley, Michal Harel

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 TolA is located in the inner membrane and comprises of three domains: the N-terminal domain I (TolAI), from residues 1-47 including a 20-residue hydrophobic membrane spanning region which anchors the protein to the cytoplasmic membrane<ref>PMID: 7853390</ref>; domain II (TolAII), from residues 48-301, which forms a rigid helix connecting the domains either side of it; and the C-terminal domain III (TolAIII) from residues 302-421, which may be involved in the function of TolA by interacting with the periplasmic or outer membrane proteins, due to the tethering to domain II.<ref name='Sharyn'>PMID: 8416897</ref>
-====C-terminal Domain====
+===C-terminal Domain===
 The c-terminal domain of TolA is directly involved with the N-terminal of both [[Colicin]] and the phage minor coat gene 3 protein. <ref>PMID: 15701516</ref>
+===Comparison with TonB===
+TolA and [[TonB]] have been shown to have a common evolutionary origin: although the two proteins can undergo domain swapping, this is difficult to achieve.  Through sedimentation experiments, it has been shown that TonB is able to remain as a monomer and form a TolA-like fold, but there would be an exposed β-ribbon which would need to undergo extensive conformational changes.  TolA does have the potential to dimerise, but it is highly unlike that it will do so.  Nevertheless, the structural similarities between these two proteins clearly indicates an evolutionary relationship, even if the functional properties have divulged<ref name='Witty'> PMID: 12169623</ref>.
 ==Function==