EMD-10890
cryo-electron density map of the P140-P110 heterodimer
EMD-10890
Single-particle4.1 Å
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Map released: 24/06/2020
Last modified: 22/05/2024
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
Sample: P140-P110 heterodimer
Fitted models: 6yrk (Avg. Q-score: 0.206)
Deposition Authors: Scheffer MP
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Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
Aparicio D
,
Scheffer MP
,
Marcos-Silva M
,
Vizarraga D
,
Sprankel L,
Ratera M
,
Weber MS
,
Seybert A,
Torres-Puig S
,
Gonzalez-Gonzalez L
,
Reitz J
,
Querol E,
Pinol J
,
Pich OQ
,
Fita I,
Frangakis AS
(2020) Nat Commun , 11 , 2877 - 2877
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(2020) Nat Commun , 11 , 2877 - 2877
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.
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.