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TitleStructural characterization of the NAP; the major adhesion complex of the human pathogen Mycoplasma genitalium.
Journal, issue, pagesMol Microbiol, Vol. 105, Issue 6, Page 869-879, Year 2017
Publish dateJul 17, 2017
AuthorsMargot P Scheffer / Luis Gonzalez-Gonzalez / Anja Seybert / Mercè Ratera / Michael Kunz / José M Valpuesta / Ignacio Fita / Enrique Querol / Jaume Piñol / Jaime Martín-Benito / Achilleas S Frangakis /
PubMed AbstractMycoplasma genitalium, the causative agent of non-gonococcal urethritis and pelvic inflammatory disease in humans, is a small eubacterium that lacks a peptidoglycan cell wall. On the surface of its ...Mycoplasma genitalium, the causative agent of non-gonococcal urethritis and pelvic inflammatory disease in humans, is a small eubacterium that lacks a peptidoglycan cell wall. On the surface of its plasma membrane is the major surface adhesion complex, known as NAP that is essential for adhesion and gliding motility of the organism. Here, we have performed cryo-electron tomography of intact cells and detergent permeabilized M. genitalium cell aggregates, providing sub-tomogram averages of free and cell-attached NAPs respectively, revealing a tetrameric complex with two-fold rotational (C2) symmetry. Each NAP has two pairs of globular lobes (named α and β lobes), arranged as a dimer of heterodimers with each lobe connected by a stalk to the cell membrane. The β lobes are larger than the α lobes by 20%. Classification of NAPs showed that the complex can tilt with respect to the cell membrane. A protein complex containing exclusively the proteins P140 and P110, was purified from M. genitalium and was structurally characterized by negative-stain single particle EM reconstruction. The close structural similarity found between intact NAPs and the isolated P140/P110 complexes, shows that dimers of P140/P110 heterodimers are the only components of the extracellular region of intact NAPs in M. genitalium.
External linksMol Microbiol / PubMed:28671286
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution19.0 - 26.0 Å
Structure data

EMDB-3753:
Negative stain 3D single particle reconstruction of the isolated surface adhesin P140/P110 complex of Mycoplasma genitalium.
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-3756:
Sub-tomogram average of the surface adhesin (NAP) complex from Mycoplasma genitalium cells by cryo-electron tomography.
Method: EM (subtomogram averaging) / Resolution: 26.0 Å

Source
  • Mycoplasma genitalium G37 (bacteria)

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