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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 385, Issue 10

Issues

X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880

Babu A. Manjasetty
  • Protein Structure Factory, c/o BESSY GmbH, Albert-Einstein-Str. 15, D-12489 Berlin, Germany and Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, D-13092 Berlin, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Frank H. Niesen
  • Protein Structure Factory, Heubnerweg 6, D-14059 Berlin, Germany and Institut für Medizinische Physik & Biophysik, Charité Universitätsmedizin Berlin, Ziegelstr. 5-9, D-10096 Berlin, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Heinrich Delbrück
  • Protein Structure Factory, Heubnerweg 6, D-14059 Berlin, Germany and Institut für Chemie/Kristallographie, Freie Universität Berlin, Takustr. 6, D-14195 Berlin, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Frank Götz
  • Protein Structure Factory, Heubnerweg 6, D-14059 Berlin, Germany and Alpha-Bioverfahrenstechnik GmbH, Heinrich-Hertz-Str. 1b, D-14532 Kleinmachnow, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Volker Sievert
  • Protein Structure Factory, Heubnerweg 6, D-14059 Berlin, Germany and Max-Planck-Institut für Molekulare Genetik, Ihnestr. 73, D-14195 Berlin, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Konrad Büssow
  • Protein Structure Factory, Heubnerweg 6, D-14059 Berlin, Germany and Max-Planck-Institut für Molekulare Genetik, Ihnestr. 73, D-14195 Berlin, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Joachim Behlke
  • Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, D-13092 Berlin, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Udo Heinemann
  • Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, D-13092 Berlin, Germany and Institut für Chemie/Kristallographie, Freie Universität Berlin, Takustr. 6, D-14195 Berlin, Germany
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Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.122

Abstract

The human protein FLJ36880 belongs to the fumarylacetoacetate hydrolase family. The X-ray structure of FLJ36880 has been determined to 2.2 Å resolution employing the semi-automated high-throughput structural genomics approach of the Protein Structure Factory. FLJ36880 adopts a mixed β-sandwich roll fold and forms homodimers in crystals as well as in solution. One Mg2+ ion is bound to each subunit of the dimeric protein by coordination to three carboxylate oxygens and three water molecules. These metal binding sites are accessible from the same surface of the dimer, partly due to the disorder of the undecapeptide stretch D29 to L39. The overall structure and metal binding site of FLJ36880 bear clear similarities to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM (Apc5008) from E. coli 1262. These similarities provide a framework for suggesting biochemical functions and evolutionary relationships of FLJ36880. It appears highly probable that the metal binding sites are involved in an enzymatic activity related to the catabolism of aromatic amino acids. Two point mutations in the active-site of FAH, responsible for the metabolic disease hereditary tyrosinemia type I (HTI) in humans, affect residues that are structurally conserved in FLJ36880 and located in the putative catalytic site.

Keywords: fumarylacetoacetate hydrolase family; hereditary tyrosinemia type I; metal-binding site; protein structure; structural genomics; X-ray crystallography

About the article

Received: April 30, 2004

Accepted: July 23, 2004

Published Online: 2005-06-01

Published in Print: 2004-10-01


Citation Information: Biological Chemistry, Volume 385, Issue 10, Pages 935–942, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.122.

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