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Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae

Type IV pili are important virulence factors on the surface of many pathogenic bacteria and have been implicated in a wide range of diverse functions, including attachment, twitching motility, biofilm formation, and horizontal gene transfer. The respiratory pathogen Streptococcus pneumoniae deploys...

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Autores principales: Muschiol, Sandra, Erlendsson, Simon, Aschtgen, Marie-Stephanie, Oliveira, Vitor, Schmieder, Peter, de Lichtenberg, Casper, Teilum, Kaare, Boesen, Thomas, Akbey, Umit, Henriques-Normark, Birgitta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5572924/
https://www.ncbi.nlm.nih.gov/pubmed/28659339
http://dx.doi.org/10.1074/jbc.M117.787671
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author Muschiol, Sandra
Erlendsson, Simon
Aschtgen, Marie-Stephanie
Oliveira, Vitor
Schmieder, Peter
de Lichtenberg, Casper
Teilum, Kaare
Boesen, Thomas
Akbey, Umit
Henriques-Normark, Birgitta
author_facet Muschiol, Sandra
Erlendsson, Simon
Aschtgen, Marie-Stephanie
Oliveira, Vitor
Schmieder, Peter
de Lichtenberg, Casper
Teilum, Kaare
Boesen, Thomas
Akbey, Umit
Henriques-Normark, Birgitta
author_sort Muschiol, Sandra
collection PubMed
description Type IV pili are important virulence factors on the surface of many pathogenic bacteria and have been implicated in a wide range of diverse functions, including attachment, twitching motility, biofilm formation, and horizontal gene transfer. The respiratory pathogen Streptococcus pneumoniae deploys type IV pili to take up DNA during transformation. These “competence pili” are composed of the major pilin protein ComGC and exclusively assembled during bacterial competence, but their biogenesis remains unclear. Here, we report the high resolution NMR structure of N-terminal truncated ComGC revealing a highly flexible and structurally divergent type IV pilin. It consists of only three α-helical segments forming a well-defined electronegative cavity and confined electronegative and hydrophobic patches. The structure is particularly flexible between the first and second α-helix with the first helical part exhibiting slightly slower dynamics than the rest of the pilin, suggesting that the first helix is involved in forming the pilus structure core and that parts of helices two and three are primarily surface-exposed. Taken together, our results provide the first structure of a type IV pilin protein involved in the formation of competence-induced pili in Gram-positive bacteria and corroborate the remarkable structural diversity among type IV pilin proteins.
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spelling pubmed-55729242017-08-29 Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae Muschiol, Sandra Erlendsson, Simon Aschtgen, Marie-Stephanie Oliveira, Vitor Schmieder, Peter de Lichtenberg, Casper Teilum, Kaare Boesen, Thomas Akbey, Umit Henriques-Normark, Birgitta J Biol Chem Microbiology Type IV pili are important virulence factors on the surface of many pathogenic bacteria and have been implicated in a wide range of diverse functions, including attachment, twitching motility, biofilm formation, and horizontal gene transfer. The respiratory pathogen Streptococcus pneumoniae deploys type IV pili to take up DNA during transformation. These “competence pili” are composed of the major pilin protein ComGC and exclusively assembled during bacterial competence, but their biogenesis remains unclear. Here, we report the high resolution NMR structure of N-terminal truncated ComGC revealing a highly flexible and structurally divergent type IV pilin. It consists of only three α-helical segments forming a well-defined electronegative cavity and confined electronegative and hydrophobic patches. The structure is particularly flexible between the first and second α-helix with the first helical part exhibiting slightly slower dynamics than the rest of the pilin, suggesting that the first helix is involved in forming the pilus structure core and that parts of helices two and three are primarily surface-exposed. Taken together, our results provide the first structure of a type IV pilin protein involved in the formation of competence-induced pili in Gram-positive bacteria and corroborate the remarkable structural diversity among type IV pilin proteins. American Society for Biochemistry and Molecular Biology 2017-08-25 2017-06-28 /pmc/articles/PMC5572924/ /pubmed/28659339 http://dx.doi.org/10.1074/jbc.M117.787671 Text en © 2017 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) .
spellingShingle Microbiology
Muschiol, Sandra
Erlendsson, Simon
Aschtgen, Marie-Stephanie
Oliveira, Vitor
Schmieder, Peter
de Lichtenberg, Casper
Teilum, Kaare
Boesen, Thomas
Akbey, Umit
Henriques-Normark, Birgitta
Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title_full Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title_fullStr Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title_full_unstemmed Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title_short Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
title_sort structure of the competence pilus major pilin comgc in streptococcus pneumoniae
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5572924/
https://www.ncbi.nlm.nih.gov/pubmed/28659339
http://dx.doi.org/10.1074/jbc.M117.787671
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