6RUT

Mycoplasma Genitalium Heterodimer Nap Complex (P140-P110 globular)

Summary for 6RUT

• Entry DOI: 10.2210/pdb6rut/pdb
• Descriptor: Mgp-operon protein 3, Adhesin P1 (3 entities in total)
• Functional Keywords: adhesion complex, sugar binding protein
• Biological source: Mycoplasma genitalium G37; More
• Total number of polymer chains: 8
• Total formula weight: 941434.44

Authors

Fita, I.,Aparicio, D. (deposition date: 2019-05-29, release date: 2020-06-24, Last modification date: 2024-01-24)

Primary citation

Aparicio, D.,Scheffer, M.P.,Marcos-Silva, M.,Vizarraga, D.,Sprankel, L.,Ratera, M.,Weber, M.S.,Seybert, A.,Torres-Puig, S.,Gonzalez-Gonzalez, L.,Reitz, J.,Querol, E.,Pinol, J.,Pich, O.Q.,Fita, I.,Frangakis, A.S.
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
Nat Commun, 11:2877-2877, 2020

PubMed 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.

PubMed: 32513917
DOI: 10.1038/s41467-020-16511-2

Experimental method

X-RAY DIFFRACTION (2.65 Å)