Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium
The adhesion complex (Nap) in Mycoplasma genitalium is composed of the adhesin proteins P110 and P140 and essential for infectivity, motility and adhesion of this human pathogen. Here, the author present the structures of P140 alone and the P140/P110 complex in closed and open conformations and base...
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Nature Portfolio
2020
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oai:doaj.org-article:1f268fe3a2fb4fb0a415fbb67e95e7822021-12-02T17:52:20ZStructure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium10.1038/s41467-020-16511-22041-1723https://doaj.org/article/1f268fe3a2fb4fb0a415fbb67e95e7822020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16511-2https://doaj.org/toc/2041-1723The adhesion complex (Nap) in Mycoplasma genitalium is composed of the adhesin proteins P110 and P140 and essential for infectivity, motility and adhesion of this human pathogen. Here, the author present the structures of P140 alone and the P140/P110 complex in closed and open conformations and based on their structural data and further functional studies propose a mechanism for the attachment and release of M. genitalium to the host cell receptor.David AparicioMargot P. SchefferMarina Marcos-SilvaDavid VizarragaLasse SprankelMercè RateraMiriam S. WeberAnja SeybertSergi Torres-PuigLuis Gonzalez-GonzalezJulian ReitzEnrique QuerolJaume PiñolOscar Q. PichIgnacio FitaAchilleas S. FrangakisNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q David Aparicio Margot P. Scheffer Marina Marcos-Silva David Vizarraga Lasse Sprankel Mercè Ratera Miriam S. Weber Anja Seybert Sergi Torres-Puig Luis Gonzalez-Gonzalez Julian Reitz Enrique Querol Jaume Piñol Oscar Q. Pich Ignacio Fita Achilleas S. Frangakis Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| description |
The adhesion complex (Nap) in Mycoplasma genitalium is composed of the adhesin proteins P110 and P140 and essential for infectivity, motility and adhesion of this human pathogen. Here, the author present the structures of P140 alone and the P140/P110 complex in closed and open conformations and based on their structural data and further functional studies propose a mechanism for the attachment and release of M. genitalium to the host cell receptor. |
| format |
article |
| author |
David Aparicio Margot P. Scheffer Marina Marcos-Silva David Vizarraga Lasse Sprankel Mercè Ratera Miriam S. Weber Anja Seybert Sergi Torres-Puig Luis Gonzalez-Gonzalez Julian Reitz Enrique Querol Jaume Piñol Oscar Q. Pich Ignacio Fita Achilleas S. Frangakis |
| author_facet |
David Aparicio Margot P. Scheffer Marina Marcos-Silva David Vizarraga Lasse Sprankel Mercè Ratera Miriam S. Weber Anja Seybert Sergi Torres-Puig Luis Gonzalez-Gonzalez Julian Reitz Enrique Querol Jaume Piñol Oscar Q. Pich Ignacio Fita Achilleas S. Frangakis |
| author_sort |
David Aparicio |
| title |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| title_short |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| title_full |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| title_fullStr |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| title_full_unstemmed |
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
| title_sort |
structure and mechanism of the nap adhesion complex from the human pathogen mycoplasma genitalium |
| publisher |
Nature Portfolio |
| publishDate |
2020 |
| url |
https://doaj.org/article/1f268fe3a2fb4fb0a415fbb67e95e782 |
| work_keys_str_mv |
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