Structure of the translocator domain of a bacterial autotransporter
| Autor: | Maya Feijen, Clasien J. Oomen, Jan Tommassen, Peter van Ulsen, Patrick Van Gelder, Piet Gros |
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| Přispěvatelé: | Kristal- en structuurchemie, Molecular Microbiology, Crystal and Structural Chemistry 1, Dep Scheikunde, Sub Molecular Microbiology, Dep Biologie, Ultrastructure, Vrije Universiteit Brussel |
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Folding Cell biology Molecular biology Molecular Sequence Data Protein Renaturation Gene Expression Neisseria meningitidis Crystallography X-Ray Microbiology Article Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Biologie/Milieukunde (BIOL) Escherichia coli Trimeric autotransporter adhesin Amino Acid Sequence Protein Structure Quaternary Molecular Biology General Immunology and Microbiology biology Membrane transport protein General Neuroscience Serine Endopeptidases Membrane Transport Proteins Life sciences Cephalosporins Protein Structure Tertiary Transport protein Protein Transport Membrane protein Biochemistry International biology.protein Autotransporter domain Biophysics Protein folding Bacterial outer membrane Protein Binding Autotransporters |
| Popis: | Autotransporters are virulence-related proteins of Gram-negative bacteria that are secreted via an outer-membrane-based C-terminal extension, the translocator domain. This domain supposedly is sufficient for the transport of the N-terminal passenger domain across the outer membrane. We present here the crystal structure of the in vitro-folded translocator domain of the autotransporter NalP from Neisseria meningitidis, which reveals a 12-stranded beta-barrel with a hydrophilic pore of 10 x 12.5 A that is filled by an N-terminal alpha-helix. The domain has pore activity in vivo and in vitro. Our data are consistent with the model of passenger-domain transport through the hydrophilic channel within the beta-barrel, and inconsistent with a model for transport through a central channel formed by an oligomer of translocator domains. However, the dimensions of the pore imply translocation of the secreted domain in an unfolded form. An alternative model, possibly covering the transport of folded domains, is that passenger-domain transport involves the Omp85 complex, the machinery required for membrane insertion of outer-membrane proteins, on which autotransporters are dependent. |
| Databáze: | OpenAIRE |
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