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2gsk
From Proteopedia
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Gene: | btuB, bfe, cer, dcrC (Escherichia coli), tonB, exbA (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 17:08:31 2008
Categories: Escherichia coli | Protein complex | Banchs, C N. | Purdy, M P. | Shultis, D D. | Wiener, M C. | CA | CNC | HEX | LDA | OCT | Beta-barrel | Membrane protein | Outer-membrane active transport | Tonb
