Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87253
Title: Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae
Authors: Muschiol, Sandra
Erlendsson, Simon
Aschtgen, Marie-Stephanie
Oliveira, Vitor
Schmieder, Peter
De Lichtenberg, Casper
Teilum, Kaare
Boesen, Thomas
Akbey, Umit
Henriques-Normark, Birgitta
Keywords: Hydrophobic Patch
Biofilm Formation
Issue Date: 2017
Source: Muschiol, S., Erlendsson, S., Aschtgen, M.-S., Oliveira, V., Schmieder, P., De Lichtenberg, C., et al. (2017). Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae. Journal of Biological Chemistry, 292(34), 14134-14146.
Series/Report no.: Journal of Biological Chemistry
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 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.
URI: https://hdl.handle.net/10356/87253
http://hdl.handle.net/10220/44346
ISSN: 0021-9258
DOI: 10.1074/jbc.M117.787671
Rights: © 2017 American Society for Biochemistry and Molecular Biology (ASBMB). This paper was published in Journal of Biological Chemistry and is made available as an electronic reprint (preprint) with permission of American Society for Biochemistry and Molecular Biology (ASBMB). The published version is available at: [http://dx.doi.org/10.1074/jbc.M117.787671]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles
SCELSE Journal Articles

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