TolR

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{{STRUCTURE_2jwk| PDB=2jwk | SIZE=400| SCENE=TolR/Tolrstructure/1 |right|CAPTION=TolR periplasmic domain dimer, [[2jwk]] }}
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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==
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'''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<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]].
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'''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<ref name='Lazzaroni'>PMID: 7853390</ref>.
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>.
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# [[Colicin A]] import
# [[Colicin A]] import
# Maintaining cell envelope integrity
# Maintaining cell envelope integrity
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</StructureSection>
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==3D structures of TolR==
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==3D structures of TolR==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[2jwk]], [[2jwl]] – TolR periplasmic domain – ''Haemophilus influenzae'' – NMR<br />
[[2jwk]], [[2jwl]] – TolR periplasmic domain – ''Haemophilus influenzae'' – NMR<br />
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[[5by4]] – TolR – ''Escherichia coli''<br />
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[[5by4]] – EcTolR – ''Escherichia coli''<br />
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[[8odt]] – EcTolR + TolQ – Cryo EM<br />
==References==
==References==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

TolR periplasmic domain dimer (PDB code 2jwk)

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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. 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
  2. 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. 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

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