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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\u2010electron tomography of intact cells and detergent permeabilized <jats:italic>M. genitalium<\/jats:italic> cell aggregates, providing sub\u2010tomogram averages of free and cell\u2010attached NAPs respectively, revealing a tetrameric complex with two\u2010fold rotational (C2) symmetry. Each NAP has two pairs of globular lobes (named \u03b1 and \u03b2 lobes), arranged as a dimer of heterodimers with each lobe connected by a stalk to the cell membrane. The \u03b2 lobes are larger than the \u03b1 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 <jats:italic>M. genitalium<\/jats:italic> and was structurally characterized by negative\u2010stain 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 <jats:italic>M. genitalium<\/jats:italic>.<\/jats:p>","DOI":"10.1111\/mmi.13743","type":"journal-article","created":{"date-parts":[[2017,7,3]],"date-time":"2017-07-03T11:53:06Z","timestamp":1499082786000},"page":"869-879","source":"Crossref","is-referenced-by-count":32,"title":["Structural characterization of the NAP; the major adhesion complex of the human pathogen <i>Mycoplasma genitalium<\/i>"],"prefix":"10.1111","volume":"105","author":[{"given":"Margot P.","family":"Scheffer","sequence":"first","affiliation":[{"name":"Buchmann Institute for Molecular Life Sciences Goethe University Frankfurt Max\u2010von\u2010Laue Str. 15 Frankfurt 60438 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