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Human NUDT18, NUDIX domain

PDB Code 3GG6 Target Class Nucleotide metabolism Target NUDT18 Alias FLJ22494, NUDT18 Disease Area/Function Date Deposited Feb 27 2009 Authors Trésaugues, L., Siponen, M.I., Lethio, L., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Moche, M., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Schueler, H., Thorsell, A.G., Van Den Berg, S., Weigelt, J., Welin, M., Wisniewska, M., Nordlund, P.

About this structure

The NUDT18 gene encodes a 323 amino-acid long protein whose function has been undiscovered so far. A NUDIX hydrolase domain [1] lies between residues 42 and 171 of NUDT18 (also known as NXR1). These domains are known to hydrolyze nucleoside diphosphate containing substrates and catalytical mechanisms have been extensively described for the representative members of this family [2].

A construct encompassing residues 26 to 177 of NUDT18 has been expressed, purified and crystallized by SGC Stockholm and let to a crystallographical structure which has been refined to 2.1Ĺ. It was solved by molecular replacement using the structure a NUDIX hydrolase from Nitrosomas europaea (PDB entry : 2B0V).

The NUDIX domain of NUDT18 is monomerical and adopts the α/β/α fold common to the other NUDIX hydrolases with a perfectly conserved NUDIX motif (GX5EX7REUXUUXGU, where U is a bulky hydrophobic residue). A supplementary three strands antiparallel β-sheet completes the structure. It lies close to the four strands mixed central β-sheet while forming together a V-shaped extended surface.

References

  1. McLennan AG. The Nudix hydrolase superfamily Cell Mol Life Sci, 2006. 63(2): p. 123-43.
  2. Mildvan AS, Xia Z, Azurmendi HF, Saraswat V, Legler PM, Massiah MA, Gabelli SB, Bianchet MA, Kang LW and Amzel LM. Structures and mechanisms of Nudix hydrolases Arch Biochem Biophys, 2005. 433(1): p. 129-43.