+検索条件
-Structure paper
タイトル | Structure of the Neisseria meningitidis Type IV pilus. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 7, Page 13015, Year 2016 |
掲載日 | 2016年10月4日 |
![]() | Subramania Kolappan / Mathieu Coureuil / Xiong Yu / Xavier Nassif / Edward H Egelman / Lisa Craig / ![]() ![]() ![]() |
PubMed 要旨 | Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin ...Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended α-helix, α1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin PilE and a ∼6 Å cryo-electron microscopy reconstruction of the intact pilus, from which we built an atomic model for the filament. This structure reveals the molecular arrangement of the N-terminal α-helices in the filament core, including a melted central portion of α1 and a bridge of electron density consistent with a predicted salt bridge necessary for pilus assembly. This structure has important implications for understanding pilus biology. |
![]() | ![]() ![]() ![]() |
手法 | EM (らせん対称) / X線回折 |
解像度 | 1.439 - 6.0 Å |
構造データ | EMDB-8287, PDB-5kua: ![]() PDB-5jw8: |
化合物 | ![]() ChemComp-HOH: |
由来 |
|
![]() | CELL ADHESION / TYPE IV PILIN / PROTEIN FIBRIL / melted helix / Type IV pili |