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TitleStructure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 2877, Year 2020
Publish dateJun 8, 2020
AuthorsDavid 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 /
PubMed AbstractMycoplasma 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 ...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.
External linksNat Commun / PubMed:32513917 / PubMed Central
MethodsEM (subtomogram averaging) / EM (single particle) / X-ray diffraction
Resolution2.65 - 15.0 Å
Structure data

EMDB-10259:
Sub-tomogram average of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
Method: EM (subtomogram averaging) / Resolution: 15.0 Å

EMDB-10260:
Structure the Nap adhesion complex from the human pathogen Mycoplasma genitalium by single particle cryo-EM.
Method: EM (single particle) / Resolution: 10.0 Å

10890

6yrk

EMDB-10890: cryo-electron density map of the P140-P110 heterodimer
PDB-6yrk: P140-P110 complex fitted into the cryo-electron density map of the heterodimer
Method: EM (single particle) / Resolution: 4.1 Å

PDB-6rut:
Mycoplasma Genitalium Heterodimer Nap Complex (P140-P110 globular)
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-6s3u:
Adhesin P140 from Mycoplasma Genitalium
Method: X-RAY DIFFRACTION / Resolution: 3.24 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mycoplasma genitalium g37 (bacteria)
  • mycoplasma genitalium (strain atcc 33530 / g-37 / nctc 10195) (bacteria)
KeywordsSUGAR BINDING PROTEIN / Adhesion complex / PROTEIN BINDING / CELL ADHESION / P110/P140 Nap Mycoplasma genitalium surface adhesin

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