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TolA | <StructureSection load='1lr0' size='350' side='right' scene='' caption='TolA domain III complex with TRIS and Zn+2 ion (grey) (PDB code [[1lr0]])'> | ||
==Structure== | |||
'''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 name='Lazzaroni'>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>. For additional details see [[Tol]]. | |||
===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 name='Deprez'>PMID: 15701516</ref>. | |||
== | ===Comparison with TonB=== | ||
TolA | 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 leaves 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== | ==Function== | ||
TolA | 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>. | ||
TolA plays an important role in the import mechanisms for the uptake of bacteriotoxins (see [[Colicin]]) and the DNA of filamentous bacteriophages<ref name='Deprez'>PMID: 15701516</ref>, and has also been shown to be involved in the bacterial sensitivity to these groups<ref name='Lazzaroni'>PMID: 7853390</ref>, in particular the alpha helix of domain II, the deletion of which causes increased cellular sensitivity to deoxycholate (a detergent)<ref name='Schendel'>PMID: 9171417</ref>. | |||
===TolA and Colicin Uptake=== | |||
Studies have shown that TolAIII plays an important role in the uptake mechanisms of colicin and DNA by being directly involved with the N-terminal of both colicin and the phage minor coat gene 3 protein<ref name='Deprez'>PMID: 15701516</ref>. | |||
== | TolA interacts with different group A colicins in different ways<ref name='Schendel'>PMID: 9171417</ref>: | ||
* [[Colicin E1]] requires different structural features of TolA to be transported than the other group A colicins, including [[Colicin E3]], [[Colicin N]] and [[Colicin A]]. Colicin E3 requires the C-terminus of TolA, which it finds with ease even when the terminus is attached very close to the membrane-spanning domain, by means of utilising a different outer membrane receptor complex to that of the other colicins | |||
* The other colicins require additional receptors in order to bind initially to the outer membrane | |||
*Colicin E1 also does not require as high of TolA levels than the other colicins in order for translocation to occur | |||
</StructureSection> | |||
==3D structures of TolA== | |||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[1lr0]] – TolA domain III – ''Pseudomonas aeruginosa''<br /> | |||
[[1s62]] – EcTolA C terminal – ''Escherichia coli'' – NMR<br /> | |||
[[2x9a]] - EcTolA C terminal + attachment protein G3P<br /> | |||
[[1tol]] - EcTolA C terminal/minor coat protein<br /> | |||
[[3qdr]] - EcTolA domain III + colicin A residues 53-107<br /> | |||
[[3qdp]] - EcTolA domain III <br /> | |||
[[6fw4]] – VcTolA C terminal – ''Vibrio cholerae'' - NMR<br /> | |||
[[4g7x]] – VcTolA C terminal + uncharacterized protein<br /> | |||
==References== | ==References== | ||
<references/> | <references/> | ||
[[Category: Topic Page]] | |||
Latest revision as of 13:32, 27 February 2020
StructureTolA 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[1]; 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[2]. For additional details see Tol. C-terminal DomainThe C-terminal domain of TolA is directly involved with the N-terminal of both Colicin and the phage minor coat gene 3 protein[3]. Comparison with TonBTolA 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 leaves 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[4]. FunctionAlthough 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[2]. TolA plays an important role in the import mechanisms for the uptake of bacteriotoxins (see Colicin) and the DNA of filamentous bacteriophages[3], and has also been shown to be involved in the bacterial sensitivity to these groups[1], in particular the alpha helix of domain II, the deletion of which causes increased cellular sensitivity to deoxycholate (a detergent)[5]. TolA and Colicin UptakeStudies have shown that TolAIII plays an important role in the uptake mechanisms of colicin and DNA by being directly involved with the N-terminal of both colicin and the phage minor coat gene 3 protein[3]. TolA interacts with different group A colicins in different ways[5]:
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3D structures of TolA3D structures of TolA
Updated on 27-February-2020
1lr0 – TolA domain III – Pseudomonas aeruginosa
1s62 – EcTolA C terminal – Escherichia coli – NMR
2x9a - EcTolA C terminal + attachment protein G3P
1tol - EcTolA C terminal/minor coat protein
3qdr - EcTolA domain III + colicin A residues 53-107
3qdp - EcTolA domain III
6fw4 – VcTolA C terminal – Vibrio cholerae - NMR
4g7x – VcTolA C terminal + uncharacterized protein
ReferencesReferences
- ↑ 1.0 1.1 Lazzaroni JC, Vianney A, Popot JL, Benedetti H, Samatey F, Lazdunski C, Portalier R, Geli V. Transmembrane alpha-helix interactions are required for the functional assembly of the Escherichia coli Tol complex. J Mol Biol. 1995 Feb 10;246(1):1-7. PMID:7853390 doi:http://dx.doi.org/10.1006/jmbi.1994.0058
- ↑ 2.0 2.1 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
- ↑ 3.0 3.1 3.2 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
- ↑ Witty M, Sanz C, Shah A, Grossmann JG, Mizuguchi K, Perham RN, Luisi B. Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein. EMBO J. 2002 Aug 15;21(16):4207-18. PMID:12169623
- ↑ 5.0 5.1 Schendel SL, Click EM, Webster RE, Cramer WA. The TolA protein interacts with colicin E1 differently than with other group A colicins. J Bacteriol. 1997 Jun;179(11):3683-90. PMID:9171417