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Human Fidgetin-like 1

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PDB Code 3D8B Target Class ATPases Target FIGNL1 Alias FIGNL1 Disease Area/Function Date Deposited May 23 2008 Authors T.KARLBERG, M.WISNIEWSKA, J.ANDERSSON, C.H.ARROWSMITH, H.BERGLUND, R.D.BUSAM, R.COLLINS, L.G.DAHLGREN, A.M.EDWARDS, S.FLODIN, A.FLORES, S.GRASLUND, M.HAMMARSTROM, A.JOHANSSON, I.JOHANSSON, A.KALLAS, T.KOTENYOVA, L.LEHTIO, M.MOCHE, M.E.NILSSON, P.NORDLUND, T.NYMAN, K.OLESEN, C.PERSSON, J.SAGEMARK, A.G.THORSELL, L.TRESAUGUES, S.VAN DEN BERG, M.WELIN, M.WIKSTROM, H.SCHULER

About this structure

Human Fidgetin-like 1 (FIGNL1) belongs to the AAA+ superfamily (ATPases associated with a variety of cellular activities). Fidgetin-like 1 is closely related to Fidgetin and Fidgetin-like 2 proteins. Mutations in the Fidgetin gene cause developmental disorders in mice. However the exact cellular functions of Fidgetin are unknown. In C. elegans the Fidgetin-like 1 homologue was observed to bind to microtubules suggesting it could be related to the AAA microtubule severing proteins Fidgetin, Spastin and Katanin.

Here, the crystal structure of the AAA-domain of human Fidgetin-like 1 is presented in complex with the nucleotide ADP at 2.0 Å resolution. The overall structure is comprised of a five-stranded parallel β–sheet flanked by &ahpha–helices that, together with a four-helix bundle, is forming the nucleotide binding pocket. The ADP was clearly seen in the electron density, however no magnesium was observed despite high concentrations in purification and crystallization conditions. The β–phosphate of ADP was seen bound to a conserved P-loop motif (GPPGTGKT). Most AAA proteins function as oligomers, usually ring-shaped hexamers; however formation of dimers in vitro has also been described in the literature. The FIGNL1 protein construct described here crystallized as a dimer.