YbgF: Difference between revisions

No edit summary
No edit summary
Line 8: Line 8:
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 invagination<ref name='Krachler'>PMID: 20816983</ref.
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 invagination<ref name='Krachler'>PMID: 20816983</ref.


It is known that YbgF interacts with the C-terminal domain of TolA during the import of colicin A into the cytoplasm<ref>PMID: 11994151</ref>.  The TPR domain in YgbF has been shown to bind to domain II in TolA, with the binding site located between residues 280-313<ref name='Gerding'>PMID: 17233825</ref>.  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.
It is known that YbgF interacts with the C-terminal domain of TolA during the import of colicin A into the cytoplasm<ref>PMID: 11994151</ref>.  The TPR domain in YgbF has been shown to bind to domain II in TolA, with the binding site located between residues 280-313<ref name='Gerding'>PMID: 17233825</ref>.  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>.


==References==
==References==
<references/>
</references>

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Laura McCauley, Michal Harel, Alexander Berchansky, Joel L. Sussman