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8PC1

Sub-tomogram average of the closed conformation of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.

Summary for 8PC1
Entry DOI10.2210/pdb8pc1/pdb
Related6R3T 6RUT 8PBX 8PBY 8PBZ 8PC0
EMDB information17587 17588 17589 17590 17591 17592 17593
DescriptorAdhesin P1, Mgp-operon protein 3 (2 entities in total)
Functional Keywordsadhesion, mycoplasma genitalium, cell adhesion
Biological sourceMycoplasmoides genitalium G37
More
Total number of polymer chains2
Total formula weight274362.51
Authors
Sprankel, L.,Scheffer, M.P.,Frangakis, A.S. (deposition date: 2023-06-09, release date: 2023-11-01, Last modification date: 2025-07-09)
Primary citationSprankel, L.,Scheffer, M.P.,Manger, S.,Ermel, U.H.,Frangakis, A.S.
Cryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.
Plos Pathog., 19:e1011761-e1011761, 2023
Cited by
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 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.
PubMed: 37939157
DOI: 10.1371/journal.ppat.1011761
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (18 Å)
Structure validation

238582

数据于2025-07-09公开中

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