TolB: Difference between revisions
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{{STRUCTURE_1c5k | PDB=1c5k | SCENE= }} | {{STRUCTURE_1c5k | PDB=1c5k | SCENE= }} | ||
==Structure== | ==Structure== | ||
TolB is a 44-kDa periplasmic protein associated with the outer membrane. It has two domains: an N-terminal α/β domain and a C-terminal six-bladed β-propeller (to which Pal and [[Colicin E9]] bind) <ref>PMID: 19696740</ref>. | |||
When Pal binds to TolB, several loops and propeller β-strands move, resulting in the latch strand of the β-propeller to move away from the dom | |||
==Function== | ==Function== | ||
==To view related Tol entries see:== | ==To view related Tol entries see:== | ||
Revision as of 10:59, 5 December 2010
Structure
TolB is a 44-kDa periplasmic protein associated with the outer membrane. It has two domains: an N-terminal α/β domain and a C-terminal six-bladed β-propeller (to which Pal and Colicin E9 bind) [1].
When Pal binds to TolB, several loops and propeller β-strands move, resulting in the latch strand of the β-propeller to move away from the dom
Function
References
- ↑ Bonsor DA, Hecht O, Vankemmelbeke M, Sharma A, Krachler AM, Housden NG, Lilly KJ, James R, Moore GR, Kleanthous C. Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins. EMBO J. 2009 Sep 16;28(18):2846-57. Epub 2009 Aug 20. PMID:19696740 doi:10.1038/emboj.2009.224
