<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Hahn E</dc:creator>
  <dc:creator>Wild P</dc:creator>
  <dc:creator>Hermanns U</dc:creator>
  <dc:creator>Sebbel P</dc:creator>
  <dc:creator>Glockshuber R</dc:creator>
  <dc:creator>Häner M</dc:creator>
  <dc:creator>Taschner N</dc:creator>
  <dc:creator>Burkhard P</dc:creator>
  <dc:creator>Aebi U</dc:creator>
  <dc:creator>Müller SA</dc:creator>
  <dc:date>2002</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">An integrated approach combining information gained by Fourier transformation, linear Markham superposition (real space) and mass-per-length measurement by scanning transmission electron microscopy was used to analyze the helical structure of the rod-like type 1 pili expressed by uropathogenic Escherichia coli strain W3110. The 3D reconstruction calculated from the experimental data showed the pili to be 6.9nm wide, right-handed helical tubes with a 19.31(+/-0.34)nm long helical repeat comprising 27 FimA monomers associated head-to-tail in eight turns of the genetic one-start helix. Adjacent turns of the genetic helix are connected via three binding sites making the pilus rod rather stiff. In situ immuno-electron microscopy experiments showed the minor subunit (FimH) mediating pilus adhesion to bladder epithelial cells to be the distal protein of the pilus tip, which had a spring-like appearance at higher magnification. The subunits FimG and FimF connect FimH to the FimA rod, the sequential orientation being FimA-FimF-FimG-FimH. The electron density map calculated at 18A resolution from an atomic model of the pilus rod (built using the pilin domain FimH together with the G1 strand of FimC as a template for FimA and applying the optimal helical parameters determined to the head-to-tail interaction model for pilus assembly) was practically identical with that of the actual 3D reconstruction.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/74913</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/s0022-2836(02)01005-7</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/12417198</dc:relation>
  <dc:source>Journal of molecular biology. - 2002</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Adhesins, Escherichia coli</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Bacterial Adhesion</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Bacterial Proteins</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Endopeptidases</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Escherichia coli</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Escherichia coli Proteins</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Fimbriae Proteins</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Fimbriae, Bacterial</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Image Processing, Computer-Assisted</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Macromolecular Substances</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Microscopy, Electron, Scanning Transmission</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Microscopy, Immunoelectron</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Models, Molecular</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Protein Subunits</dc:subject>
  <dc:subject xmlns:ns16="xml" ns16:lang="en">Virulence</dc:subject>
  <dc:title xmlns:ns17="xml" ns17:lang="en">Exploring the 3D molecular architecture of Escherichia coli type 1 pili.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
