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TitleCryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.
Journal, issue, pagesPLoS Pathog, Vol. 19, Issue 11, Page e1011761, Year 2023
Publish dateNov 8, 2023
AuthorsLasse Sprankel / Margot P Scheffer / Sina Manger / Utz H Ermel / Achilleas S Frangakis /
PubMed AbstractThe 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 linksPLoS Pathog / PubMed:37939157 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution3.3 - 18.0 Å
Structure data

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

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

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

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

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

ChemComp-HOH:
WATER

Source
  • mycoplasmoides genitalium g37 (bacteria)
KeywordsCELL ADHESION / Adhesion / Mycoplasma genitalium

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