TolR
From Proteopedia
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| - | + | <StructureSection load='' size='350' side='right' scene='TolR/Tolrstructure/1' caption='TolR periplasmic domain dimer (PDB code [[2jwk]])'> | |
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==Structure== | ==Structure== | ||
| - | TolR is a bitopic protein located in the inner membrane and consists of three domains: domain I (from residues 1 to 43 and including the transmembrane domain between residues 23 to 43), domain II and domain III from residues 117 to 142 | + | '''TolR''' is a bitopic protein (protein having a single α helix in its transmembrane domain) located in the inner membrane and consists of three domains: domain I (from residues 1 to 43 and including the transmembrane domain between residues 23 to 43), domain II and domain III from residues 117 to 142<ref name='Journet'>PMID: 10419942</ref>. Domains II and III have the ability to dimerize, but unlike domains I and III, domain II is poorly conserved<ref>PMID: 11994151</ref>. For additional details see [[Tol]]. |
| - | Domain III has been suggested to form an amphiphilic α-helix, which play an essential role in the functional assembly of the Tol complex | + | Domain III has been suggested to form an amphiphilic α-helix, which play an essential role in the functional assembly of the [[Tol]] complex<ref name='Lazzaroni'>PMID: 7853390</ref>. |
==Function== | ==Function== | ||
TolR has been shown to exhibit several functions<ref name='Journet'>PMID: 10419942</ref>: | TolR has been shown to exhibit several functions<ref name='Journet'>PMID: 10419942</ref>: | ||
| - | # Interactions with other Tol proteins: Domain I is important for the interactions between TolA and TolQ, as deletion of this domain resulted in no cross-linkages formed between these proteins | + | # Interactions with other Tol proteins: Domain I is important for the interactions between [[TolA]] and [[TolQ]], as deletion of this domain resulted in no cross-linkages formed between these proteins<ref name='Journet'>PMID: 10419942</ref>. Domain III of TolR has also been shown to be involved in the TolQ-TolR interaction, but not directly linked<ref name='Lazzaroni'>PMID: 7853390</ref>. However, even when deleted there is still cross linking between TolR and TolQ showing that domain III does not affect the interaction between the two proteins, but could instead affect the function of TolR<ref name='Journet'>PMID: 10419942</ref>. As domain III has not been shown to interact directly with TolA or TolQ, the function of TolR could be affected ''indirectly'' by domain III altering the conformation of domain I thereby affecting the interaction between TolA/TolQ-TolR. |
| - | # Colicin A import | + | # [[Colicin A]] import |
# Maintaining cell envelope integrity | # Maintaining cell envelope integrity | ||
| + | </StructureSection> | ||
| + | ==3D structures of TolR== | ||
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| + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
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| + | [[2jwk]], [[2jwl]] – TolR periplasmic domain – ''Haemophilus influenzae'' – NMR<br /> | ||
| + | [[5by4]] – EcTolR – ''Escherichia coli''<br /> | ||
| + | [[8odt]] – EcTolR + TolQ – Cryo EM<br /> | ||
==References== | ==References== | ||
<references/> | <references/> | ||
| + | [[Category:Topic Page]] | ||
Current revision
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3D structures of TolR
Updated on 27-December-2023
2jwk, 2jwl – TolR periplasmic domain – Haemophilus influenzae – NMR
5by4 – EcTolR – Escherichia coli
8odt – EcTolR + TolQ – Cryo EM
References
- ↑ 1.0 1.1 1.2 1.3 Journet L, Rigal A, Lazdunski C, Benedetti H. Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ. J Bacteriol. 1999 Aug;181(15):4476-84. PMID:10419942
- ↑ Walburger A, Lazdunski C, Corda Y. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol Microbiol. 2002 May;44(3):695-708. PMID:11994151
- ↑ 3.0 3.1 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
