Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.
Journal, issue, pages	PLoS Pathog, Vol. 19, Issue 11, Page e1011761, Year 2023
Publish date	Nov 8, 2023
Authors	Lasse Sprankel / Margot P Scheffer / Sina Manger / Utz H Ermel / Achilleas S Frangakis /
PubMed Abstract	The nap particle is an immunogenic surface adhesion complex from Mycoplasma genitalium. It is essential for motility and responsible for binding sialylated oligosaccharides on the surface of the host ...The nap particle is an immunogenic surface adhesion complex from Mycoplasma genitalium. It is essential for motility and responsible for binding sialylated oligosaccharides on the surface of the host cell. The nap particle is composed of two P140-P110 heterodimers, the structure of which was recently solved. However, the interpretation of the mechanism by which the mycoplasma cells orchestrate adhesion remained challenging. Here, we provide cryo-electron tomography structures at ~11 Å resolution, which allow for the distinction between the bound and released state of the nap particle, displaying the in vivo conformational states. Fitting of the atomically resolved structures reveals that bound sialylated oligosaccharides are stabilized by both P110 and P140. Movement of the stalk domains allows for the transfer of conformational changes from the interior of the cell to the binding pocket, thus having the capability of an active release process. It is likely that the same mechanism can be transferred to other Mycoplasma species that belong to the pneumoniae cluster.
External links	PLoS Pathog / PubMed:37939157 / PubMed Central
Methods	EM (single particle) / EM (subtomogram averaging)
Resolution	3.3 - 18.0 Å
Structure data	17587 8pbx EMDB-17587, PDB-8pbx: Single particle cryo-EM of the P140-P110 heterodimer of Mycoplasma genitalium at 3.3 Angstrom resolution. Method: EM (single particle) / Resolution: 3.3 Å 17588 8pby EMDB-17588, PDB-8pby: Single particle cryo-EM of the P140-P110 heterodimer with an alternative conformation in the P140 stalk of Mycoplasma genitalium at a resolution of 3.7 Angstrom. Method: EM (single particle) / Resolution: 3.7 Å EMDB-17589: Single particle cryo-EM of the Nap complex of Mycoplasma genitalium in the expanded conformation at 7.3 Angstrom resolution. Method: EM (single particle) / Resolution: 7.3 Å EMDB-17590: Single particle cryo-EM of the Nap adhesion complex of Mycoplasma genitalium in the canonical conformation at 8.3 Angstrom resolution. Method: EM (single particle) / Resolution: 8.3 Å 17591 8pbz EMDB-17591, PDB-8pbz: Sub-tomogram average of the Nap adhesion complex from the human pathogen Mycoplasma genitalium at 11 Angstrom. Method: EM (subtomogram averaging) / Resolution: 11.0 Å 17592 8pc0 EMDB-17592, PDB-8pc0: Sub-tomogram average of the open conformation of the Nap adhesion complex from the human pathogen Mycoplasma genitalium. Method: EM (subtomogram averaging) / Resolution: 17.0 Å 17593 8pc1 EMDB-17593, PDB-8pc1: Sub-tomogram average of the closed conformation of the Nap adhesion complex from the human pathogen Mycoplasma genitalium. Method: EM (subtomogram averaging) / Resolution: 18.0 Å EMDB-18414: Single particle cryo-EM of the Nap adhesion complex of Mycoplasma genitalium soaked with 6'-SL at 7.7 Angstrom resolution. Method: EM (single particle) / Resolution: 7.7 Å
Chemicals	ChemComp-K: Unknown entry ChemComp-PO4: PHOSPHATE ION / Phosphate ChemComp-HOH: WATER / Water
Source	mycoplasmoides genitalium g37 (bacteria)
Keywords	CELL ADHESION / Adhesion / Mycoplasma genitalium