2GSK

Structure of the BtuB:TonB Complex

Summary for 2GSK

• Entry DOI: 10.2210/pdb2gsk/pdb
• Descriptor: Vitamin B12 transporter btuB, protein TONB, CALCIUM ION, ... (8 entities in total)
• Functional Keywords: outer-membrane active transport, beta-barrel, tonb, membrane protein, signaling protein-membrane protein complex, signaling protein/membrane protein
• Biological source: Escherichia coli; More
• Cellular location: Cell outer membrane ; Multi- pass membrane protein : P06129
• Total number of polymer chains: 2
• Total formula weight: 78071.67

Authors

Shultis, D.D.,Purdy, M.P.,Banchs, C.N.,Wiener, M.C. (deposition date: 2006-04-26, release date: 2006-06-13, Last modification date: 2023-08-30)

Primary citation

Shultis, D.D.,Purdy, M.D.,Banchs, C.N.,Wiener, M.C.
Outer membrane active transport: structure of the BtuB:TonB complex
Science, 312:1396-1399, 2006

PubMed Abstract: 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.

PubMed: 16741124
DOI: 10.1126/science.1127694

Experimental method

X-RAY DIFFRACTION (2.1 Å)