TolB: Difference between revisions
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TolB has been shown to be essential for the function of the Tol system in ''Escherichia coli''<ref>PMID: 19696740</ref>. | TolB has been shown to be essential for the function of the Tol system in ''Escherichia coli''<ref>PMID: 19696740</ref>. | ||
{{STRUCTURE_1crz | PDB= | {{STRUCTURE_1crz | PDB=1crz | SCENE= }} | ||
==Structure== | ==Structure== | ||
Revision as of 16:19, 30 January 2011
TolB has been shown to be essential for the function of the Tol system in Escherichia coli[1].
StructureStructure
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) [2].
When Pal binds to TolB, several loops and propeller β-strands move, resulting in the latch strand of the β-propeller to move away.
FunctionFunction
Related Tol entriesRelated Tol entries
ReferencesReferences
- ↑ 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
- ↑ 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