TonB

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The BtuB-[[TonB]] complex is involved in the uptake of essential nutrients from outside the cell across the outer membrane.
The BtuB-[[TonB]] complex is involved in the uptake of essential nutrients from outside the cell across the outer membrane.
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TonB attaches to BtuB on the periplasmic side of the 614 amino acid BtuB protein <ref name=name='Shultis'> PMID: 16741124</ref>
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TonB attaches to BtuB on the periplasmic side of the 614 amino acid BtuB protein <ref name='Shultis'> PMID: 16741124</ref>
==Function==
==Function==

Revision as of 09:18, 25 April 2011

Template:STRUCTURE 1xx3

TonB is involved in the uptake of iron as a component of the TonB/ExbB/ExbD complex of the Ton system.

Contents

Structure

TonB and ExbD bind to ExbB in a protein complex that prevents the degradation of the TonB protein. TonB and ExbD are anchored to the cytoplasmic membrane via their N-terminal hydrophobic sequences, with the rest of the protein complex extending into the periplasmic space, allowing for interaction with outer membrane proteins.[1]

BtuB-TonB Complex

Template:STRUCTURE 2gsk

TonB complexes with BtuB in order to aid the transport of nutrients across the outer membrane by incorporating the proton-motive force into the outer membrane.[2]

The BtuB-TonB complex is involved in the uptake of essential nutrients from outside the cell across the outer membrane.

TonB attaches to BtuB on the periplasmic side of the 614 amino acid BtuB protein [2]

Function

The activity of TonB is determined by the presence of ExbB and ExbD. [1]

Regulation

References

  1. 1.0 1.1 Kampfenkel K, Braun V. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J Biol Chem. 1993 Mar 15;268(8):6050-7. PMID:8449962
  2. 2.0 2.1 Shultis DD, Purdy MD, Banchs CN, Wiener MC. Outer membrane active transport: structure of the BtuB:TonB complex. Science. 2006 Jun 2;312(5778):1396-9. PMID:16741124 doi:312/5778/1396

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Michal Harel, Laura McCauley

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