YbgF
Template:STRUCTURE 2xev Template:STRUCTURE 2wz7
StructureStructure
YbgF is a periplasmic protein with an N-terminal coiled coil domain (NTD) 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, as seen in 2XEV. This connection can be cleaved by proteases[2].
FunctionFunction
Although YbgF is conserved in most gram-negative organisms, the exact function of this protein is still unknown. It may be involved in the late stages of cell division when the Tol complex is recruited to the area of septation, or also during invaginationCite error: Closing </ref> missing for <ref> tag. The TPR domain in YgbF has been shown to bind to domain II in TolA, with the binding site located between residues 280-313[1]. The NTD is not directly involved with the binding to TolA, but is important for the transition of YbgF in its oligomeric state when binding to TolA. This may be due to the NTD restricting the formation of the trimer state, allowing the TPR to bind with TolA<ref name='Krachler'>PMID: 20816983</ref.
ReferencesReferences
- ↑ 1.0 1.1 1.2 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
- ↑ 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