Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae

Sandra Muschiol; Simon Erlendsson; Marie-Stephanie Aschtgen; Vitor Oliveira; Peter Schmieder; Casper de Lichtenberg; Kaare Teilum; Thomas Boesen; Umit Akbey; Birgitta Henriques-Normark

doi:10.1074/jbc.M117.787671

Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae

Sandra Muschiol, Simon Erlendsson, Marie-Stephanie Aschtgen, Vitor Oliveira, Peter Schmieder, Casper de Lichtenberg, Kaare Teilum, Thomas Boesen, Umit Akbey, Birgitta Henriques-Normark

Biomolecular Sciences

16 Citations (Scopus)

51 Downloads (Pure)

Abstract

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 proteinComGCand 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.

Original language	English
Journal	Journal of Biological Chemistry
Volume	292
Issue number	34
Pages (from-to)	14134-14146
Number of pages	13
ISSN	0021-9258
DOIs	https://doi.org/10.1074/jbc.M117.787671
Publication status	Published - 25 Aug 2017

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title = "Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae",

abstract = "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 proteinComGCand 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.",

author = "Sandra Muschiol and Simon Erlendsson and Marie-Stephanie Aschtgen and Vitor Oliveira and Peter Schmieder and {de Lichtenberg}, Casper and Kaare Teilum and Thomas Boesen and Umit Akbey and Birgitta Henriques-Normark",

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T1 - Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae

AU - Muschiol, Sandra

AU - Erlendsson, Simon

AU - Aschtgen, Marie-Stephanie

AU - Oliveira, Vitor

AU - Schmieder, Peter

AU - de Lichtenberg, Casper

AU - Teilum, Kaare

AU - Boesen, Thomas

AU - Akbey, Umit

AU - Henriques-Normark, Birgitta

PY - 2017/8/25

Y1 - 2017/8/25

N2 - 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 proteinComGCand 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.

AB - 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 proteinComGCand 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.

U2 - 10.1074/jbc.M117.787671

DO - 10.1074/jbc.M117.787671

M3 - Journal article

C2 - 28659339

SN - 0021-9258

VL - 292

SP - 14134

EP - 14146

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 34

ER -

Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae

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