TolA
TolA is located in the inner membrane, anchored by its domain I.
StructureStructure
TolA comprises of three domains: domain I, from residues 1-47 including a 20-residue hydrophobic membrane spanning region; domain II, from residues 48-301, which forms a rigid helix connecting the domains either side of it; and domain III 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.[1]
FunctionFunction
TolA plays an important role in the import mechanisms for the uptake of bacteriotoxins (see Colicin) and the DNA of filamentous bacteriophages.[2]
Although the exact function of TolA is not yet known, it has been shown that unlike mutations in the proteins of the TonB system to which the TolQRA proteins show many similarities, mutations in the TolQRA proteins affect the outer membrane integrity. TolA could be involved structurally by bringing the inner and outer membranes together and forming a bridge or link between them.[1]
The c-terminal domain of TolA is directly involved with the N-terminal of both Colicin and the phage minor coat gene 3 protein. [3]
ReferencesReferences
- ↑ 1.0 1.1 Levengood-Freyermuth SK, Click EM, Webster RE. Role of the carboxyl-terminal domain of TolA in protein import and integrity of the outer membrane. J Bacteriol. 1993 Jan;175(1):222-8. PMID:8416897
- ↑ Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L. Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain. J Mol Biol. 2005 Mar 4;346(4):1047-57. Epub 2005 Jan 12. PMID:15701516 doi:10.1016/j.jmb.2004.12.028
- ↑ Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L. Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain. J Mol Biol. 2005 Mar 4;346(4):1047-57. Epub 2005 Jan 12. PMID:15701516 doi:10.1016/j.jmb.2004.12.028