DOI: 10.1073/pnas.0509620103. Structure and assembly of P-pili: A protruding hinge region used for assembly of a bacterial adhesion filament

Structure and assembly of P-pili: A protruding hinge region used for assembly of a bacterial adhesion filament

10.1073/pnas.0509620103

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

High-resolution structures of macromolecular complexes offer unparalleled insight into the workings of biological systems and hence the interplay of these systems in health and disease. We have adopted a multifaceted approach to understanding the pathogenically important structure of P-pili, the class I adhesion pili from pyelonephritic Escherichia coli . Our approach combines electron cryomicroscopy, site-directed mutagenesis, homology modeling, and energy calculations, resulting in a high-resolution model of PapA, the major structural element of these pili. Fitting of the modeled PapA subunit into the electron cryomicroscopy data provides a detailed view of these pilins within the supramolecular architecture of the pilus filament. A structural hinge in the N-terminal region of the subunit is located at the site of a newly resolved electron density that protrudes from the P-pilus surface. The structural flexibility provided by this hinge is necessary for assembly of P-pili, illustrating one solution to construction of large macromolecular complexes from small repeating units. These data support our hypothesis that domain-swapped pilin subunits transit the outer cell membrane vertically and rotate about the hinge for final positioning into the pilus filament. Our data confirm and supply a structural basis for much previous genetic, biochemical, and structural data. This model of the P-pilus filament provides an insight into the mechanism of assembly of a macromolecular complex essential for initiation of kidney infection by these bacteria.

Bibliography

Mu, X.-Q., & Bullitt, E. (2006). Structure and assembly of P-pili: A protruding hinge region used for assembly of a bacterial adhesion filament. Proceedings of the National Academy of Sciences, 103(26), 9861â9866.

Authors 2

Xiang-Qi Mu (first)
Esther Bullitt (additional)

References 32 Referenced 63

Dates

Type	When
Created	19 years, 2 months ago (June 16, 2006, 9:16 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 2:13 p.m.)
Indexed	3 months, 4 weeks ago (May 3, 2025, 1:07 p.m.)
Issued	19 years, 2 months ago (June 27, 2006)
Published	19 years, 2 months ago (June 27, 2006)
Published Online	19 years, 2 months ago (June 27, 2006)
Published Print	19 years, 2 months ago (June 27, 2006)

Funders 0

None

BibTeX

@article{Mu_2006, title={Structure and assembly of P-pili: A protruding hinge region used for assembly of a bacterial adhesion filament}, volume={103}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0509620103}, DOI={10.1073/pnas.0509620103}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Mu, Xiang-Qi and Bullitt, Esther}, year={2006}, month=jun, pages={9861–9866} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        5,
        3
      ]
    ],
    "date-time": "2025-05-03T17:07:05Z",
    "timestamp": 1746292025568
  },
  "reference-count": 32,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "26",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        2006,
        6,
        27
      ]
    ]
  },
  "abstract": "<jats:p>\n            High-resolution structures of macromolecular complexes offer unparalleled insight into the workings of biological systems and hence the interplay of these systems in health and disease. We have adopted a multifaceted approach to understanding the pathogenically important structure of P-pili, the class I adhesion pili from pyelonephritic\n            <jats:italic>Escherichia coli</jats:italic>\n            . Our approach combines electron cryomicroscopy, site-directed mutagenesis, homology modeling, and energy calculations, resulting in a high-resolution model of PapA, the major structural element of these pili. Fitting of the modeled PapA subunit into the electron cryomicroscopy data provides a detailed view of these pilins within the supramolecular architecture of the pilus filament. A structural hinge in the N-terminal region of the subunit is located at the site of a newly resolved electron density that protrudes from the P-pilus surface. The structural flexibility provided by this hinge is necessary for assembly of P-pili, illustrating one solution to construction of large macromolecular complexes from small repeating units. These data support our hypothesis that domain-swapped pilin subunits transit the outer cell membrane vertically and rotate about the hinge for final positioning into the pilus filament. Our data confirm and supply a structural basis for much previous genetic, biochemical, and structural data. This model of the P-pilus filament provides an insight into the mechanism of assembly of a macromolecular complex essential for initiation of kidney infection by these bacteria.\n          </jats:p>",
  "DOI": "10.1073/pnas.0509620103",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        6,
        17
      ]
    ],
    "date-time": "2006-06-17T01:16:25Z",
    "timestamp": 1150506985000
  },
  "page": "9861-9866",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 63,
  "title": "Structure and assembly of P-pili: A protruding hinge region used for assembly of a bacterial adhesion filament",
  "prefix": "10.1073",
  "volume": "103",
  "author": [
    {
      "given": "Xiang-Qi",
      "family": "Mu",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118"
        }
      ]
    },
    {
      "given": "Esther",
      "family": "Bullitt",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118"
        }
      ]
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        2006,
        6,
        27
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_3_3_1_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1099/00222615-1-1-45"
    },
    {
      "key": "e_1_3_3_2_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1099/00222615-4-4-467"
    },
    {
      "key": "e_1_3_3_3_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.91.25.11889"
    },
    {
      "key": "e_1_3_3_4_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1146/annurev.mi.45.100191.002123"
    },
    {
      "key": "e_1_3_3_5_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.2164-0947.1965.tb02342.x"
    },
    {
      "key": "e_1_3_3_6_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/373164a0"
    },
    {
      "key": "e_1_3_3_7_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.93.21.11913"
    },
    {
      "key": "e_1_3_3_8_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1365-2958.1992.tb01399.x"
    },
    {
      "key": "e_1_3_3_9_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/iai.41.3.942-949.1983"
    },
    {
      "key": "e_1_3_3_10_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.83.6.1891"
    },
    {
      "key": "e_1_3_3_11_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/iai.59.11.3849-3858.1991"
    },
    {
      "key": "e_1_3_3_12_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.157.1.330-333.1984"
    },
    {
      "key": "e_1_3_3_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.285.5430.1061"
    },
    {
      "key": "e_1_3_3_14_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.285.5430.1058"
    },
    {
      "key": "e_1_3_3_15_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0092-8674(02)01050-4"
    },
    {
      "key": "e_1_3_3_16_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/nature03916"
    },
    {
      "key": "e_1_3_3_17_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.str.2005.01.005"
    },
    {
      "key": "e_1_3_3_18_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0304-3991(00)00062-0"
    },
    {
      "key": "e_1_3_3_19_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/prot.340230306"
    },
    {
      "key": "e_1_3_3_20_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1107/S0907444998003254"
    },
    {
      "key": "e_1_3_3_21_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.175.23.7639-7643.1993"
    },
    {
      "key": "e_1_3_3_22_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.85.4.1247"
    },
    {
      "key": "e_1_3_3_23_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.93.23.12890"
    },
    {
      "key": "e_1_3_3_24_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/emboj/17.21.6155"
    },
    {
      "key": "e_1_3_3_25_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.jmb.2004.11.037"
    },
    {
      "key": "e_1_3_3_26_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1993.tb05724.x"
    },
    {
      "key": "e_1_3_3_27_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(92)90860-M"
    },
    {
      "key": "e_1_3_3_28_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1993.1170"
    },
    {
      "key": "e_1_3_3_29_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/jcc.540160303"
    },
    {
      "key": "e_1_3_3_30_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1107/S0907444998008208"
    },
    {
      "key": "e_1_3_3_31_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(76)90004-8"
    },
    {
      "key": "e_1_3_3_32_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jsbi.1996.0030"
    }
  ],
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.0509620103",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        12
      ]
    ],
    "date-time": "2022-04-12T18:13:05Z",
    "timestamp": 1649787185000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.0509620103"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2006,
        6,
        27
      ]
    ]
  },
  "references-count": 32,
  "journal-issue": {
    "issue": "26",
    "published-print": {
      "date-parts": [
        [
          2006,
          6,
          27
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.0509620103"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.0509620103",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        2006,
        6,
        27
      ]
    ]
  },
  "assertion": [
    {
      "value": "2005-11-04",
      "order": 0,
      "name": "received",
      "label": "Received",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    },
    {
      "value": "2006-06-27",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}