Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium
| Autor: | Margot P. Scheffer, Miriam S. Weber, Merce Ratera, Marina Marcos-Silva, Enrique Querol, Luis González-González, Ignacio Fita, Anja Seybert, Jaume Piñol, Sergi Torres-Puig, Oscar Q. Pich, David Aparicio, Julian Reitz, David Vizarraga, Achilleas S. Frangakis, Lasse Sprankel |
|---|---|
| Přispěvatelé: | Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), German Research Foundation, Ministerio de Economía y Competitividad (España) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
animal structures Science 030106 microbiology Protein domain General Physics and Astronomy Mycoplasma genitalium Sialic acid binding Crystallography X-Ray Microbiology Article Bacterial Adhesion Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Structure-Activity Relationship 03 medical and health sciences Bacterial Proteins Protein Domains Cryoelectron microscopy Pelvic inflammatory disease Humans Binding site lcsh:Science X-ray crystallography Infectivity Binding Sites Multidisciplinary biology Chemistry General Chemistry biology.organism_classification Cell biology Bacterial adhesin Nap 030104 developmental biology Mutation Cryoelectron tomography lcsh:Q Protein Multimerization Pathogens |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020) Dipòsit Digital de Documents de la UAB Universitat Autònoma de Barcelona Digital.CSIC. Repositorio Institucional del CSIC instname Nature Communications |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|