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2014-03-21Zeitschriftenartikel DOI: 10.1107/S1399004714001606
The type IV secretion protein TraK from the Enterococcus conjugative plasmid pIP501 exhibits a novel fold
dc.contributor.authorGoessweiner-Mohr, Nikolaus
dc.contributor.authorFercher, Christian
dc.contributor.authorArends, Karsten
dc.contributor.authorGruenberger, Ruth Birner-
dc.contributor.authorGomez, Diana Laverde-
dc.contributor.authorHuebner, Johannes
dc.contributor.authorGrohmann, Elisabeth
dc.contributor.authorKeller, Walter
dc.date.accessioned2018-05-07T18:25:59Z
dc.date.available2018-05-07T18:25:59Z
dc.date.created2015-08-25
dc.date.issued2014-03-21none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/re33RagFHAQeg/PDF/22bXGeeawJJY.pdf
dc.identifier.urihttp://edoc.rki.de/176904/2122
dc.description.abstractConjugative 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 multiprotein 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 TraK was determined to 3.0 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.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut
dc.subjectTraKeng
dc.subject4hiceng
dc.subject.ddc610 Medizin
dc.titleThe type IV secretion protein TraK from the Enterococcus conjugative plasmid pIP501 exhibits a novel fold
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10040710
dc.identifier.doi10.1107/S1399004714001606
dc.identifier.doihttp://dx.doi.org/10.25646/2047
local.edoc.container-titleActa Crystallographica Section D Biological Crystallography
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://journals.iucr.org/d/issues/2014/04/00/mn5045/index.html
local.edoc.container-publisher-nameInternational Union of Crystallography
local.edoc.container-volumeD70
local.edoc.container-year2014

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