TolA

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==Structure==
==Structure==
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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>
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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 (see [[TolA C-Termainal Domain]]) 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==

Revision as of 13:25, 14 February 2011

TolA is located in the inner membrane, anchored by its domain I.

Contents

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 (see TolA C-Termainal Domain) 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]

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.[1]

To view related Tol entries see:

References

  1. 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

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Michal Harel, Laura McCauley

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