YbgF
YbgF is a periplasmic protein which interacts with the C-terminal domain of TolA (TolAIII) during the import of colicin A into the cytoplasm. [2]
StructureStructure
YbgF is a periplasmic protein with an N-terminal coiled coil domain (NTD) (see 3D structure 2XEV) and a C-terminal tetratricopeptide domain (TPR), both of which are autonomous[1]. As seen in the 3D structure 2WZ7, the NTD forms an elongated trimer which is connected via a flexible linker to the TPR trimer. This connection can be cleaved by proteases[3].
FunctionFunction
ReferencesReferences
- ↑ 1.0 1.1 Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA. 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. coli. Mol Microbiol. 2007 Feb;63(4):1008-25. PMID:17233825 doi:10.1111/j.1365-2958.2006.05571.x
- ↑ 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
- ↑ Krachler AM, Sharma A, Cauldwell A, Papadakos G, Kleanthous C. TolA modulates the oligomeric status of YbgF in the bacterial periplasm. J Mol Biol. 2010 Oct 22;403(2):270-85. Epub 2010 Sep 15. PMID:20816983 doi:10.1016/j.jmb.2010.08.050