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Página principal > Artículos > Artículos publicados > Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium |
Fecha: | 2020 |
Resumen: | Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9. 8 and 15 Å, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of M. genitalium to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity. |
Ayudas: | Ministerio de Economía y Competitividad BFU2018-101265-B-100 Agencia Estatal de Investigación BIO2017-84166-R Ministerio de Economía y Competitividad MDM-2014-0435 |
Derechos: | Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. |
Lengua: | Anglès |
Documento: | Article ; recerca ; Versió publicada |
Materia: | Cryoelectron microscopy ; Cryoelectron tomography ; Microbiology ; Pathogens ; X-ray crystallography |
Publicado en: | Nature communications, Vol. 11 (June 2020) , art. 2877, ISSN 2041-1723 |
10 p, 3.5 MB |