TolB

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{{STRUCTURE_1c5k | PDB=1c5k | SCENE= }}
{{STRUCTURE_1c5k | PDB=1c5k | SCENE= }}
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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>.
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==Structure==
==Structure==
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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>.
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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==
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When TolB
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==To view related Tol entries see:==
==To view related Tol entries see:==

Revision as of 10:59, 5 December 2010

Template:STRUCTURE 1c5k


Contents

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

To view related Tol entries see:


References

  1. 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Laura McCauley, Joel L. Sussman

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