Bacteria of the genus Mycoplasma lack obvious homologs of prokaryotic or eukaryotic cytoskeletal, as well as motility-related genes (except FtsZ). Nevertheless, they maintain characteristic cell shapes and show adhesion and gliding abilities on both artificial surfaces and cells. Earlier genetic, biochemical, and electron microscopic analyses have shown that the tip structure, located at the tapered end of gliding mycoplasmas, is indispensable for this behavior. In this study, we have analyzed the fine structure of the Mycoplasma pneumoniae tip by cryo-electron tomography. We show that the central rod is surrounded by quasi-periodical electron-dense macromolecular complexes. Additional complexes are located at the distal end of the rod which connect the rod to the cytoplasmic membrane. Furthermore, we detect a structure at the proximal end of the rod that attaches the rod to the cell membrane. The surface protein complexes have been mapped in detail and their distribution on the cell surface has been visualized. Since the rod structures were detected at a close to native state of the cells, they allow us to build a hypothesis describing the motility mechanism of M. pneumoniae. Finally, we have evaluated the ribosome density of the organism by a template matching approach, whereby the reliability of the detection was supported by a comparative bioinformatics analysis.