Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Goessweiner-Mohr, N; Fercher, C; Arends, K; Birner-Gruenberger, R; Laverde-Gomez, D; Huebner, J; Grohmann, E; Keller, W.
The type IV secretion protein TraK from the Enterococcus conjugative plasmid pIP501 exhibits a novel fold.
Acta Crystallogr D Biol Crystallogr. 2014; 70(Pt 4):1124-1135
Doi: 10.1107/S1399004714001606
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- Co-Autor*innen der Med Uni Graz
- Birner-Grünberger Ruth
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- Abstract:
- Conjugative plasmid transfer presents a serious threat to human health as the most important means of spreading antibiotic resistance and virulence genes among bacteria. The required direct cell-cell contact is established by a multi-protein complex, the conjugative type IV secretion system (T4SS). The conjugative core complex spans the cellular envelope and serves as a channel for macromolecular secretion. T4SSs of Gram-negative (G-) origin have been studied in great detail. In contrast, T4SSs of Gram-positive (G+) bacteria have only received little attention thus far, despite the medical relevance of numerous G+ pathogens (e.g. enterococci, staphylococci and streptococci). This study provides structural information on the type IV secretion (T4S) protein TraK of the G+ broad host range Enterococcus conjugative plasmid pIP501. The crystal structure of the N-terminally truncated construct TraKΔ was determined to 3.0 Å resolution and exhibits a novel fold. Immunolocalization demonstrated that the protein localizes to the cell wall facing towards the cell exterior, but does not exhibit surface accessibility. Circular dichroism, dynamic light scattering and size-exclusion chromatography confirmed the protein to be a monomer. With the exception of proteins from closely related T4SSs, no significant sequence or structural relatives were found. This observation marks the protein as a very exclusive, specialized member of the pIP501 T4SS.
- Find related publications in this database (using NLM MeSH Indexing)
- Bacterial Proteins - chemistry
- Bacterial Proteins - genetics
- Bacterial Proteins - metabolism
- DNA-Binding Proteins - chemistry
- DNA-Binding Proteins - genetics
- DNA-Binding Proteins - metabolism
- Enterococcus faecalis - chemistry
- Enterococcus faecalis - genetics
- Enterococcus faecalis - metabolism
- Models, Molecular -
- Plasmids - chemistry
- Plasmids - metabolism
- Protein Structure, Tertiary -