EMD-10890

Single-particle
4.1 Å
EMD-10890 Deposition: 20/04/2020
Map released: 24/06/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10890

cryo-electron density map of the P140-P110 heterodimer

EMD-10890

Single-particle
4.1 Å
EMD-10890 Deposition: 20/04/2020
Map released: 24/06/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Sample: P140-P110 heterodimer
Fitted models: 6yrk (Avg. Q-score: 0.206)

Deposition Authors: Scheffer MP , Aparicio D
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
PUBMED: 32513917
DOI: doi:10.1038/s41467-020-16511-2
ISSN: 2041-1723
Abstract:
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.