Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution

Jacqueline L. Hilsenbeck, Hajeung Park, Gregory Chen, Buhyun Youn, Kathleen Postle, Chul Hee Kang

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Colicin B (55 kDa) is a cytotoxic protein that recognizes the outer membrane transporter, FepA, as a receptor and, after gaining access to the cytoplasmic membranes of sensitive Escherichia coli cells, forms a pore that depletes the electrochemical potential of the membrane and ultimately results in cell death. To begin to understand the series of dynamic conformational changes that must occur as colicin B translocates from outer membrane to cytoplasmic membrane, we report here the crystal structure of colicin B at 2.5 Å resolution. The crystal belongs to the space group C2221 with unit cell dimensions a=132.162 Å, b=138.167 Å, c=106.16 Å. The overall structure of colicin B is dumbbell shaped. Unlike colicin Ia, the only other TonB-dependent colicin crystallized to date, colicin B does not have clearly structurally delineated receptor-binding and translocation domains. Instead, the unique N-terminal lobe of the dumbbell contains both domains and consists of a large (290 residues), mostly β-stranded structure with two short α-helices. This is followed by a single long (≈ 74 Å) helix that connects the N-terminal domain to the C-terminal pore-forming domain, which is composed of 10 α-helices arranged in a bundle-type structure, similar to the pore-forming domains of other colicins. The TonB box sequence at the N-terminus folds back to interact with the N-terminal lobe of the dumbbell and leaves the flanking sequences highly disordered. Comparison of sequences among many colicins has allowed the identification of a putative receptor-binding domain.

Original languageEnglish (US)
Pages (from-to)711-720
Number of pages10
JournalMolecular Microbiology
Volume51
Issue number3
DOIs
StatePublished - Feb 1 2004

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Colicins
Bacterial Proteins
Cell Membrane
IgA receptor
Membrane Transport Proteins
Membrane Potentials
Cell Death
Escherichia coli

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Hilsenbeck, Jacqueline L. ; Park, Hajeung ; Chen, Gregory ; Youn, Buhyun ; Postle, Kathleen ; Kang, Chul Hee. / Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution. In: Molecular Microbiology. 2004 ; Vol. 51, No. 3. pp. 711-720.
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Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution. / Hilsenbeck, Jacqueline L.; Park, Hajeung; Chen, Gregory; Youn, Buhyun; Postle, Kathleen; Kang, Chul Hee.

In: Molecular Microbiology, Vol. 51, No. 3, 01.02.2004, p. 711-720.

Research output: Contribution to journalArticle

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AU - Hilsenbeck, Jacqueline L.

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