TolA: Difference between revisions
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TolA | TolA is located in the inner membrane, anchored by its domain I. | ||
==Structure== | ==Structure== | ||
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.<ref name='Sharyn'>PMID: 8416897</ref> | 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.<ref name='Sharyn'>PMID: 8416897</ref> | ||
==Function== | ==Function== | ||
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.<ref name='Sharyn'>PMID: 8416897</ref> | |||
==To view related Tol entries see:== | ==To view related Tol entries see:== | ||
*[[Tol]] | *[[Tol]] | ||
Revision as of 16:18, 14 February 2011
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
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]