5NCA

Solution structure of ComGC from Streptococcus pneumoniae

5NCA の概要

• エントリーDOI: 10.2210/pdb5nca/pdb
• NMR情報: BMRB: 34112
• 分子名称: Competence protein ComGC (1 entity in total)
• 機能のキーワード: comgc, pilin, type iv pilin, streptococcus pneumoniae type iv competence pilin, structural protein
• 由来する生物種: Streptococcus pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7697.50

構造登録者

Erlendsson, S.,Schmeider, P.,Lichtenberg, C.,Teilum, K.,Akbey, U. (登録日: 2017-03-03, 公開日: 2017-07-05, 最終更新日: 2024-06-19)

主引用文献

Muschiol, S.,Erlendsson, S.,Aschtgen, M.S.,Oliveira, V.,Schmieder, P.,de Lichtenberg, C.,Teilum, K.,Boesen, T.,Akbey, U.,Henriques-Normark, B.
Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae.
J. Biol. Chem., 292:14134-14146, 2017

PubMed 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 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.

PubMed: 28659339
DOI: 10.1074/jbc.M117.787671

実験手法

SOLUTION NMR