View in EDS PDF Full Text

Atomic model of the type III secretion system needle.

Saved in:
Bibliographic Details
Title: Atomic model of the type III secretion system needle.
Authors: Loquet, Antoine, Sgourakis, Nikolaos G., Gupta, Rashmi, Giller, Karin, Riedel, Dietmar, Goosmann, Christian, Griesinger, Christian, Kolbe, Michael, Baker, David, Becker, Stefan, Lange, Adam
Source: Nature. 6/14/2012, Vol. 486 Issue 7402, p276-279. 4p. 2 Diagrams, 1 Graph.
Subjects: Atomic models, Secretion, Pathogenic bacteria, Infection, Eukaryotic cells
Abstract: Pathogenic bacteria using a type III secretion system (T3SS) to manipulate host cells cause many different infections including Shigella dysentery, typhoid fever, enterohaemorrhagic colitis and bubonic plague. An essential part of the T3SS is a hollow needle-like protein filament through which effector proteins are injected into eukaryotic host cells. Currently, the three-dimensional structure of the needle is unknown because it is not amenable to X-ray crystallography and solution NMR, as a result of its inherent non-crystallinity and insolubility. Cryo-electron microscopy combined with crystal or solution NMR subunit structures has recently provided a powerful hybrid approach for studying supramolecular assemblies, resulting in low-resolution and medium-resolution models. However, such approaches cannot deliver atomic details, especially of the crucial subunit-subunit interfaces, because of the limited cryo-electron microscopic resolution obtained in these studies. Here we report an alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle. We show that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns, similar to that of the flagellar filament of S. typhimurium. In contrast to established models of the needle in which the amino terminus of the protein subunit was assumed to be ?-helical and positioned inside the needle, our model reveals an extended amino-terminal domain that is positioned on the surface of the needle, while the highly conserved carboxy terminus points towards the lumen. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: pbh
DbLabel: Psychology and Behavioral Sciences Collection
An: 76575589
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Atomic model of the type III secretion system needle.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Loquet%2C+Antoine%22">Loquet, Antoine</searchLink><br /><searchLink fieldCode="AR" term="%22Sgourakis%2C+Nikolaos+G%2E%22">Sgourakis, Nikolaos G.</searchLink><br /><searchLink fieldCode="AR" term="%22Gupta%2C+Rashmi%22">Gupta, Rashmi</searchLink><br /><searchLink fieldCode="AR" term="%22Giller%2C+Karin%22">Giller, Karin</searchLink><br /><searchLink fieldCode="AR" term="%22Riedel%2C+Dietmar%22">Riedel, Dietmar</searchLink><br /><searchLink fieldCode="AR" term="%22Goosmann%2C+Christian%22">Goosmann, Christian</searchLink><br /><searchLink fieldCode="AR" term="%22Griesinger%2C+Christian%22">Griesinger, Christian</searchLink><br /><searchLink fieldCode="AR" term="%22Kolbe%2C+Michael%22">Kolbe, Michael</searchLink><br /><searchLink fieldCode="AR" term="%22Baker%2C+David%22">Baker, David</searchLink><br /><searchLink fieldCode="AR" term="%22Becker%2C+Stefan%22">Becker, Stefan</searchLink><br /><searchLink fieldCode="AR" term="%22Lange%2C+Adam%22">Lange, Adam</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 6/14/2012, Vol. 486 Issue 7402, p276-279. 4p. 2 Diagrams, 1 Graph.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Atomic+models%22">Atomic models</searchLink><br /><searchLink fieldCode="DE" term="%22Secretion%22">Secretion</searchLink><br /><searchLink fieldCode="DE" term="%22Pathogenic+bacteria%22">Pathogenic bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Infection%22">Infection</searchLink><br /><searchLink fieldCode="DE" term="%22Eukaryotic+cells%22">Eukaryotic cells</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Pathogenic bacteria using a type III secretion system (T3SS) to manipulate host cells cause many different infections including Shigella dysentery, typhoid fever, enterohaemorrhagic colitis and bubonic plague. An essential part of the T3SS is a hollow needle-like protein filament through which effector proteins are injected into eukaryotic host cells. Currently, the three-dimensional structure of the needle is unknown because it is not amenable to X-ray crystallography and solution NMR, as a result of its inherent non-crystallinity and insolubility. Cryo-electron microscopy combined with crystal or solution NMR subunit structures has recently provided a powerful hybrid approach for studying supramolecular assemblies, resulting in low-resolution and medium-resolution models. However, such approaches cannot deliver atomic details, especially of the crucial subunit-subunit interfaces, because of the limited cryo-electron microscopic resolution obtained in these studies. Here we report an alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle. We show that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns, similar to that of the flagellar filament of S. typhimurium. In contrast to established models of the needle in which the amino terminus of the protein subunit was assumed to be ?-helical and positioned inside the needle, our model reveals an extended amino-terminal domain that is positioned on the surface of the needle, while the highly conserved carboxy terminus points towards the lumen. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=76575589
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1038/nature11079
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 4
        StartPage: 276
    Subjects:
      – SubjectFull: Atomic models
        Type: general
      – SubjectFull: Secretion
        Type: general
      – SubjectFull: Pathogenic bacteria
        Type: general
      – SubjectFull: Infection
        Type: general
      – SubjectFull: Eukaryotic cells
        Type: general
    Titles:
      – TitleFull: Atomic model of the type III secretion system needle.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Loquet, Antoine
      – PersonEntity:
          Name:
            NameFull: Sgourakis, Nikolaos G.
      – PersonEntity:
          Name:
            NameFull: Gupta, Rashmi
      – PersonEntity:
          Name:
            NameFull: Giller, Karin
      – PersonEntity:
          Name:
            NameFull: Riedel, Dietmar
      – PersonEntity:
          Name:
            NameFull: Goosmann, Christian
      – PersonEntity:
          Name:
            NameFull: Griesinger, Christian
      – PersonEntity:
          Name:
            NameFull: Kolbe, Michael
      – PersonEntity:
          Name:
            NameFull: Baker, David
      – PersonEntity:
          Name:
            NameFull: Becker, Stefan
      – PersonEntity:
          Name:
            NameFull: Lange, Adam
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 14
              M: 06
              Text: 6/14/2012
              Type: published
              Y: 2012
          Identifiers:
            – Type: issn-print
              Value: 00280836
          Numbering:
            – Type: volume
              Value: 486
            – Type: issue
              Value: 7402
          Titles:
            – TitleFull: Nature
              Type: main
ResultId 1