View in EDS PDF Full Text

Structure of the E. coli protein-conducting channel bound to a translating ribosome.

Saved in:
Bibliographic Details
Title: Structure of the E. coli protein-conducting channel bound to a translating ribosome.
Authors: Mitra, Kakoli, Schaffitzel, Christiane, Shaikh, Tanvir, Tama, Florence, Jenni, Simon, Brooks III, Charles L., Ban, Nenad, Frank, Joachim
Source: Nature. 11/17/2005, Vol. 438 Issue 7066, p318-324. 7p. 4 Diagrams.
Subjects: Escherichia coli, Escherichia, Gram-negative bacteria, Membrane proteins, Proteins, RNA, Ribose
Abstract: Secreted and membrane proteins are translocated across or into cell membranes through a protein-conducting channel (PCC). Here we present a cryo-electron microscopy reconstruction of the Escherichia coli PCC, SecYEG, complexed with the ribosome and a nascent chain containing a signal anchor. This reconstruction shows a messenger RNA, three transfer RNAs, the nascent chain, and detailed features of both a translocating PCC and a second, non-translocating PCC bound to mRNA hairpins. The translocating PCC forms connections with ribosomal RNA hairpins on two sides and ribosomal proteins at the back, leaving a frontal opening. Normal mode-based flexible fitting of the archaeal SecYEβ structure into the PCC electron microscopy densities favours a front-to-front arrangement of two SecYEG complexes in the PCC, and supports channel formation by the opening of two linked SecY halves during polypeptide translocation. On the basis of our observation in the translocating PCC of two segregated pores with different degrees of access to bulk lipid, we propose a model for co-translational protein translocation. [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: 18893111
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Structure of the E. coli protein-conducting channel bound to a translating ribosome.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Mitra%2C+Kakoli%22">Mitra, Kakoli</searchLink><br /><searchLink fieldCode="AR" term="%22Schaffitzel%2C+Christiane%22">Schaffitzel, Christiane</searchLink><br /><searchLink fieldCode="AR" term="%22Shaikh%2C+Tanvir%22">Shaikh, Tanvir</searchLink><br /><searchLink fieldCode="AR" term="%22Tama%2C+Florence%22">Tama, Florence</searchLink><br /><searchLink fieldCode="AR" term="%22Jenni%2C+Simon%22">Jenni, Simon</searchLink><br /><searchLink fieldCode="AR" term="%22Brooks+III%2C+Charles+L%2E%22">Brooks III, Charles L.</searchLink><br /><searchLink fieldCode="AR" term="%22Ban%2C+Nenad%22">Ban, Nenad</searchLink><br /><searchLink fieldCode="AR" term="%22Frank%2C+Joachim%22">Frank, Joachim</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 11/17/2005, Vol. 438 Issue 7066, p318-324. 7p. 4 Diagrams.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia%22">Escherichia</searchLink><br /><searchLink fieldCode="DE" term="%22Gram-negative+bacteria%22">Gram-negative bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Membrane+proteins%22">Membrane proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22RNA%22">RNA</searchLink><br /><searchLink fieldCode="DE" term="%22Ribose%22">Ribose</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Secreted and membrane proteins are translocated across or into cell membranes through a protein-conducting channel (PCC). Here we present a cryo-electron microscopy reconstruction of the Escherichia coli PCC, SecYEG, complexed with the ribosome and a nascent chain containing a signal anchor. This reconstruction shows a messenger RNA, three transfer RNAs, the nascent chain, and detailed features of both a translocating PCC and a second, non-translocating PCC bound to mRNA hairpins. The translocating PCC forms connections with ribosomal RNA hairpins on two sides and ribosomal proteins at the back, leaving a frontal opening. Normal mode-based flexible fitting of the archaeal SecYEβ structure into the PCC electron microscopy densities favours a front-to-front arrangement of two SecYEG complexes in the PCC, and supports channel formation by the opening of two linked SecY halves during polypeptide translocation. On the basis of our observation in the translocating PCC of two segregated pores with different degrees of access to bulk lipid, we propose a model for co-translational protein translocation. [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=18893111
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1038/nature04133
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 7
        StartPage: 318
    Subjects:
      – SubjectFull: Escherichia coli
        Type: general
      – SubjectFull: Escherichia
        Type: general
      – SubjectFull: Gram-negative bacteria
        Type: general
      – SubjectFull: Membrane proteins
        Type: general
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: RNA
        Type: general
      – SubjectFull: Ribose
        Type: general
    Titles:
      – TitleFull: Structure of the E. coli protein-conducting channel bound to a translating ribosome.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Mitra, Kakoli
      – PersonEntity:
          Name:
            NameFull: Schaffitzel, Christiane
      – PersonEntity:
          Name:
            NameFull: Shaikh, Tanvir
      – PersonEntity:
          Name:
            NameFull: Tama, Florence
      – PersonEntity:
          Name:
            NameFull: Jenni, Simon
      – PersonEntity:
          Name:
            NameFull: Brooks III, Charles L.
      – PersonEntity:
          Name:
            NameFull: Ban, Nenad
      – PersonEntity:
          Name:
            NameFull: Frank, Joachim
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 17
              M: 11
              Text: 11/17/2005
              Type: published
              Y: 2005
          Identifiers:
            – Type: issn-print
              Value: 00280836
          Numbering:
            – Type: volume
              Value: 438
            – Type: issue
              Value: 7066
          Titles:
            – TitleFull: Nature
              Type: main
ResultId 1