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'''Structure of the BtuB:TonB Complex''' | '''Structure of the BtuB:TonB Complex''' | ||
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[[Category: Shultis, D D.]] | [[Category: Shultis, D D.]] | ||
[[Category: Wiener, M C.]] | [[Category: Wiener, M C.]] | ||
[[Category: | [[Category: Beta-barrel]] | ||
[[Category: | [[Category: Membrane protein]] | ||
[[Category: | [[Category: Outer-membrane active transport]] | ||
[[Category: | [[Category: Tonb]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:28:34 2008'' | |||
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Revision as of 02:28, 4 May 2008
Structure of the BtuB:TonB Complex
Overview
In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport.
About this Structure
2GSK is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Outer membrane active transport: structure of the BtuB:TonB complex., Shultis DD, Purdy MD, Banchs CN, Wiener MC, Science. 2006 Jun 2;312(5778):1396-9. PMID:16741124 Page seeded by OCA on Sun May 4 05:28:34 2008
