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PDBsum entry 4hic
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Unknown function
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PDB id
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4hic
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References listed in PDB file
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Key reference
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Title
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The type IV secretion protein trak from the enterococcus conjugative plasmid pip501 exhibits a novel fold.
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Authors
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N.Goessweiner-Mohr,
C.Fercher,
K.Arends,
R.Birner-Gruenberger,
D.Laverde-Gomez,
J.Huebner,
E.Grohmann,
W.Keller.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2014,
70,
1124-1135.
[DOI no: ]
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PubMed id
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Abstract
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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.
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