Mapping the interactions between escherichia coli tol subunits: rotation of the TolR transmembrane helix.

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Mapping the interactions between escherichia coli tol subunits: rotation of the TolR transmembrane helix. is …
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scholarly articleQ13442814

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P356DOI10.1074/JBC.M805257200
P698PubMed publication ID19075020

P50authorEric CascalesQ56513758
Roland LloubesQ61827019
P2093author name stringMarthe Gavioli
Emilie L Goemaere
Xiang Y-Z Zhang
Rémi Thomé
P2860cites workColicin biologyQ24671701
The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteinsQ27648743
The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS dataQ27649836
The bacterial flagellar motor: structure and function of a complex molecular machineQ28252092
A slow-motility phenotype caused by substitutions at residue Asp31 in the PomA channel component of a sodium-driven flagellar motorQ30870475
The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity?Q34334962
The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coliQ35596402
Membrane topology of the Escherichia coli TolR protein required for cell envelope integrityQ36122421
Mutant MotB proteins in Escherichia coliQ36148108
Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coliQ36238659
The tol gene products and the import of macronmolecules into Escherichia coliQ36533420
Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR.Q39504085
Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrityQ39694516
Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activityQ39841349
Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segmentQ39929505
Conformational change in the stator of the bacterial flagellar motorQ43774060
Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator ComplexQ43774063
Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA.Q43967562
The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB.Q43982260
Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB.Q45951699
New pUC-derived cloning vectors with different selectable markers and DNA replication originsQ48230311
Movements of the TolR C-terminal domain depend on TolQR ionizable key residues and regulate activity of the Tol complex.Q54442978
Mutational analyses define helix organization and key residues of a bacterial membrane energy-transducing complex.Q54448529
Deletion analyses of the peptidoglycan-associated lipoprotein Pal reveals three independent binding sequences including a TolA box.Q54512173
Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins.Q54612317
Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli.Q54612320
Transmembrane alpha-helix interactions are required for the functional assembly of the Escherichia coli Tol complex.Q54617237
P433issue7
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
transmembrane proteinQ424204
P304page(s)4275-4282
P577publication date2008-12-15
P1433published inJournal of Biological ChemistryQ867727
P1476titleMapping the interactions between escherichia coli tol subunits: rotation of the TolR transmembrane helix
P478volume284