Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium
Aparicio Alarcón, David (Institut de Biologia Molecular de Barcelona)
Scheffer, Margot P. (Buchmann Institute for Molecular Life Sciences)
Marcos Silva, Marina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Vizarraga, David (Institut de Biologia Molecular de Barcelona)
Sprankel, Lasse (Buchmann Institute for Molecular Life Sciences)
Ratera, Mercè (Institut de Biologia Molecular de Barcelona)
Weber, Miriam S. (Buchmann Institute for Molecular Life Sciences)
Seybert, Anja (Buchmann Institute for Molecular Life Sciences)
Torres Puig, Sergi (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Gonzalez-Gonzalez, Luis 1987- (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Reitz, Julian (Buchmann Institute for Molecular Life Sciences)
Querol Murillo, Enrique (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Piñol Ribas, Jaume (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Quijada Pich, Oscar (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Fita, Ignacio (Institut de Biologia Molecular de Barcelona)
Frangakis, Achilleas S. (Buchmann Institute for Molecular Life Sciences)

Date:	2020
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.
Grants:	Ministerio de Economía y Competitividad BFU2018-101265-B-100 Agencia Estatal de Investigación BIO2017-84166-R Ministerio de Economía y Competitividad MDM-2014-0435
Rights:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Language:	Anglès
Document:	Article ; recerca ; Versió publicada
Subject:	Cryoelectron microscopy ; Cryoelectron tomography ; Microbiology ; Pathogens ; X-ray crystallography
Published in:	Nature communications, Vol. 11 (June 2020) , art. 2877, ISSN 2041-1723

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

10 p, 3.5 MB

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Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Research articles
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