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The structure and function for the majority of these effector proteins remains unknown. Here, we present the crystal structure of the <jats:italic>L. pneumophila<\/jats:italic> effector Lem10. The structure reveals a multidomain organization with the largest C\u2010terminal domain showing strong structural similarity to the HD protein superfamily representatives. However, Lem10 lacks the catalytic His\u2010Asp residue pair and does not show any <jats:italic>in vitro<\/jats:italic> phosphohydrolase enzymatic activity, typical for HD proteins. While the biological function of Lem10 remains elusive, our analysis shows that similar distinct features are shared by a significant number of HD domains found in <jats:italic>Legionella<\/jats:italic> proteins, including the SidE family of effectors known to play an important role during infection. Taken together our data point to the presence of a specific group of non\u2010catalytic <jats:italic>Legionella<\/jats:italic> HD domains, dubbed LHDs, which are involved in pathogenesis. Proteins 2015; 83:2319\u20132325. \u00a9 2015 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/prot.24933","type":"journal-article","created":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T21:30:47Z","timestamp":1443735047000},"page":"2319-2325","source":"Crossref","is-referenced-by-count":5,"title":["Crystal structure of the <i>Legionella pneumophila<\/i> lem10 effector reveals a new member of the <scp>HD<\/scp> protein superfamily"],"prefix":"10.1002","volume":"83","author":[{"given":"Mariya","family":"Morar","sequence":"first","affiliation":[{"name":"Department of Chemical Engineering and Applied Chemistry University of Toronto  Ontario Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elena","family":"Evdokimova","sequence":"additional","affiliation":[{"name":"Department of Chemical Engineering and Applied Chemistry University of Toronto  Ontario 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