| Range |
~20 nm
|
| Organism |
Bacteria Escherichia coli |
| Reference |
De Geyter J et al., Protein folding in the cell envelope of Escherichia coli. Nat Microbiol. 2016 Jul 26 1(8):16107. doi: 10.1038/nmicrobiol.2016.107 p.6 right column top paragraphPubMed ID27573113
|
| Primary Source |
[82] Krojer T et al., Structural basis for the regulated protease and chaperone function of DegP. Nature. 2008 Jun 12 453(7197):885-90. doi: 10.1038/nature07004PubMed ID18496527
|
| Comments |
P.6 right column top paragraph: "The overall diameter of the 24-subunit DegP (~20 nm) (Fig. 3d) approaches the distance between the PM (plasma membrane) and OM (outer membrane), suggesting the simultaneous interaction of projecting PDZ domains with both membranes for safe client transit directly to the OM (primary source)." Wiki: "The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals." |
| Entered by |
Uri M |
| ID |
114124 |