P0ABV6: Tol-Pal system protein TolR (tolR)

Tol-Pal system protein TolR (tolR) is a 142-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0ABV6.

Gene
tolR
Organism
Escherichia coli (strain K12)
Length
142 residues
Mean pLDDT
79.0
Model
AF-P0ABV6-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.0 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate13%
70 to 90Confident: backbone generally right59%
50 to 70Low: treat with caution28%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:11722743). The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726). The system also appears to be required for the activity of several outer membrane-localized enzymes with cell wall remodeling activity (PubMed:32152098). Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to…

Subunit structure

The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer (PubMed:17233825). TolR forms homodimers (PubMed:10419942, PubMed:26354441). Interacts with the N-terminal domain of TolA and with TolQ…

Subcellular location

Cell inner membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5BY4X-ray1.7 ÅA=36-142
9O40EM2.92 ÅF/G=1-142
9DDMEM2.94 ÅY/Z=1-142
9DDNEM3.18 ÅY/Z=1-142
9KPZEM3.18 ÅF/G=1-142
9QUQEM3.28 ÅF/G=1-142
9QVDEM3.52 ÅF/G=1-142
9K49EM3.6 ÅF/G=1-142
9KQ0EM3.6 ÅF/G=1-142
9KCHEM4.19 ÅF/G=1-142
8ODTEM4.2 ÅF/G=1-142

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