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  X-ray structure of Fumarylacetoacetate Hydrolase(FAH) family member Homo sapiens FLJ36880

Manjasetty, B. A., Niesen, F. H., Delbrueck, H., Goetz, F., Sievert, V., Buessow, K., et al. (2004). X-ray structure of Fumarylacetoacetate Hydrolase(FAH) family member Homo sapiens FLJ36880. Biological Chemistry, 385(10), 935-942. doi:10.1515/BC.2004.122.

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Genre: Journal Article
Alternative Title : Biol. Chem.

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 Creators:
Manjasetty, Babu A., Author
Niesen, Frank H., Author
Delbrueck, Heinrich, Author
Goetz, Frank, Author
Sievert, Volker1, Author           
Buessow, Konrad1, Author           
Behlke, Joachim, Author
Heinemann, Udo, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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Free keywords: fumarylacetoacetate hydrolase family, hereditary tyrosinemia type I, metal-binding site, protein structure, structural genomics, X-ray crystallography.
 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.

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Language(s): eng - English
 Dates: 2004-10-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 229894
DOI: 10.1515/BC.2004.122
 Degree: -

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Title: Biological Chemistry
  Alternative Title : Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 385 (10) Sequence Number: - Start / End Page: 935 - 942 Identifier: ISSN: 1431-6730