umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Structural and functional characterization of shaft, anchor, and tip proteins of the Mfa1 fimbria from the periodontal pathogen Porphyromonas gingivalis
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, article id 1793Article in journal (Refereed) Published
Abstract [en]

Very little is known about how fimbriae of Bacteroidetes bacteria are assembled. To shed more light on this process, we solved the crystal structures of the shaft protein Mfa1, the regulatory protein Mfa2, and the tip protein Mfa3 from the periodontal pathogen Porphyromonas gingivalis. Together these build up part of the Mfa1 fimbria and represent three of the five proteins, Mfa1-5, encoded by the mfa1 gene cluster. Mfa1, Mfa2 and Mfa3 have the same overall fold i.e., two β-sandwich domains. Upon polymerization, the first β-strand of the shaft or tip protein is removed by indigenous proteases. Although the resulting void is expected to be filled by a donor-strand from another fimbrial protein, the mechanism by which it does so is still not established. In contrast, the first β-strand in Mfa2, the anchoring protein, is firmly attached by a disulphide bond and is not cleaved. Based on the structural information, we created multiple mutations in P. gingivalis and analysed their effect on fimbrial polymerization and assembly in vivo. Collectively, these data suggest an important role for the C-terminal tail of Mfa1, but not of Mfa3, affecting both polymerization and maturation of downstream fimbrial proteins.

Place, publisher, year, edition, pages
2018. Vol. 8, article id 1793
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-144501DOI: 10.1038/s41598-018-20067-zISI: 000423430400005PubMedID: 29379120OAI: oai:DiVA.org:umu-144501DiVA, id: diva2:1180152
Available from: 2018-02-05 Created: 2018-02-05 Last updated: 2018-06-09Bibliographically approved

Open Access in DiVA

fulltext(5073 kB)82 downloads
File information
File name FULLTEXT01.pdfFile size 5073 kBChecksum SHA-512
1de60895fc497ee918dcd8879a07a917fcb48bbae389ed3a0c98628c2854dad66f52f48147bae5b1a3ce7da86e67b5c03cd8457934ad3ee492ccf9a845655411
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Hall, MichaelPersson, Karina

Search in DiVA

By author/editor
Hall, MichaelPersson, Karina
By organisation
Department of Chemistry
In the same journal
Scientific Reports
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 82 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 225 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf