YbgF
From Proteopedia
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==Structure== | ==Structure== | ||
'''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<ref name='Gerding'>PMID: 17233825</ref>. As seen in the <scene name='42/429024/Cv/1'>3D structure 2WZ7</scene>, the NTD forms an elongated trimer which is connected via a flexible linker to the TPR trimer, <scene name='42/429024/Cv/2'>as seen in 2XEV</scene>. This connection can be cleaved by proteases<ref name='Krachler'>PMID: 20816983</ref>. | '''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<ref name='Gerding'>PMID: 17233825</ref>. As seen in the <scene name='42/429024/Cv/1'>3D structure 2WZ7</scene>, the NTD forms an elongated trimer which is connected via a flexible linker to the TPR trimer, <scene name='42/429024/Cv/2'>as seen in 2XEV</scene>. This connection can be cleaved by proteases<ref name='Krachler'>PMID: 20816983</ref>. | ||
Revision as of 07:56, 15 December 2016
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References
- ↑ 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
- ↑ 2.0 2.1 2.2 2.3 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
- ↑ 3.0 3.1 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
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