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Human tRNA-specific adenosine-34 deaminase subunit ADAT2

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PDB Code 3DH1 Target Class Nucleotide metabolism Target DEADC1 Alias n/a Disease Area/Function Date Deposited Jun 17 2008 Authors M.WELIN, L.TRESAUGUES, J.ANDERSSON, C.H.ARROWSMITH, H.BERGLUND, R.COLLINS, L.G.DAHLGREN, A.M.EDWARDS, S.FLODIN, A.FLORES, S.GRASLUND, M.HAMMARSTROM, A.JOHANSSON, I.JOHANSSON, T.KARLBERG, T.KOTENYOVA, L.LEHTIO, M.MOCHE, M.E.NILSSON, T.NYMAN, K.OLESEN, C.PERSSON, J.SAGEMARK, H.SCHUELER, A.G.THORSELL, L.TRESAUGUES, S.VAN DEN BERG, M.WISNIEWSKA, M.WIKSTROM, P.NORDLUND

About this structure

DEADC1A (Deaminase domain-containing protein 1) or ADAT2 (adenosine deaminase acting on tRNA) is a deaminase editing the adenosine at the wobble position (pos 34) in tRNAs. The adenosine is post-transcriptionally deaminated to an inosine, giving mature tRNAs. In prokaryotes this reaction is catalyzed by tadA which acts as homodimers, while in eukaryotes this is performed by a heterodimer built up by ADAT2-ADAT3 [2]. Inosine at position 34 is thought to play a critical part in protein synthesis, which is consistent with that both the tadA and ADAT2-ADAT3 genes are crucial for cell viability [2]. ADAT2 has three zinc ligands and a glutamic acid that is needed for proton transfer, while the ADAT3 is missing the glutamic acid suggesting that ADAT2 is the catalytical subunit [1,2].

Here we have determined the structure of the human tRNA-specific adenosine-34 deaminase, subunit ADAT2 to a resolution of 2.8 Å. The structure was solved using molecular replacement with the structure of a tRNA-specific adenosine deaminase from Streptococcus pyogenes (pdb-code: 2NX8) as a search model. There is one zinc ion bound to each subunit, coordinated by two cysteines, one histidine and one water molecule. The asymmetric unit consists of four molecules, building up two dimers with the same dimer interface as previous bacterial structures [3,4,5].

References

  1. Schaub M, Keller W. Biochimie. 2002 Aug;84(8):791-803.
  2. Gerber AP, Keller W. Science. 1999 Nov 5;286(5442):1146-9.
  3. Losey HC, Ruthenburg AJ, Verdine GL. Nat Struct Mol Biol. 2006 Feb;13(2):153-9.
  4. Kuratani M et. al. J Biol Chem. 2005 Apr 22;280(16):16002-8.
  5. Lee WH et. al. Proteins. 2007 Sep 1;68(4):1016-9.