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We describe here the structure and biochemistry of a complex between the Rab-binding domain of LidA and active Rab8a. LidA displays structural peculiarities in binding to Rab8a, forming a considerably extended interface in comparison to known mammalian Rab effectors, and involving regions of the GTPase that are not seen in other Rab:effector complexes. In keeping with this extended binding interface, which involves four \u03b1-helices and two pillar-like structures of LidA, the stability of LidA-Rab interactions is dramatically greater than for other such complexes. For Rab1b and Rab8a, these affinities are extraordinarily high, but for the more weakly bound Rab6a,\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    values of 4\u00a0nM for the inactive and 30\u00a0pM for the active form were found. Rab1b and Rab8a appear to bind LidA with\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    values in the low picomolar range, making LidA a Rab supereffector.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1113133108","type":"journal-article","created":{"date-parts":[[2011,10,20]],"date-time":"2011-10-20T00:47:37Z","timestamp":1319071657000},"page":"17945-17950","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":82,"title":["Protein LidA from Legionella is a Rab GTPase supereffector"],"prefix":"10.1073","volume":"108","author":[{"given":"Stefan","family":"Schoebel","sequence":"first","affiliation":[{"name":"Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam L.","family":"Cichy","sequence":"additional","affiliation":[{"name":"Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roger S.","family":"Goody","sequence":"additional","affiliation":[{"name":"Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aymelt","family":"Itzen","sequence":"additional","affiliation":[{"name":"Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,10,19]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.semcdb.2010.10.003","article-title":"GTPases involved in vesicular trafficking: Structures and mechanisms","volume":"22","author":"Itzen A","year":"2011","unstructured":"A Itzen, RS Goody, GTPases involved in vesicular trafficking: Structures and mechanisms. 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