6IYM

Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum

Summary for 6IYM

• Entry DOI: 10.2210/pdb6iym/pdb
• Descriptor: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: fumarylacetoacetate hydrolase, exiguobacterium antarctica, hydrolase
• Biological source: Exiguobacterium antarcticum B7
• Total number of polymer chains: 2
• Total formula weight: 63240.02

Authors

Lee, J.H.,Lee, C.W. (deposition date: 2018-12-17, release date: 2019-04-03, Last modification date: 2024-03-27)

Primary citation

Yoo, W.,Lee, C.W.,Kim, B.Y.,Huong Luu Le, L.T.,Park, S.H.,Kim, H.W.,Shin, S.C.,Kim, K.K.,Lee, J.H.,Kim, T.D.
Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.
Biochem. Biophys. Res. Commun., 509:773-778, 2019

PubMed Abstract: Fumarylacetoacetate hydrolase (FAH) is essential for the degradation of aromatic amino acids as well as for the cleavage of carbon-carbon bonds in metabolites or small organic compounds. Here, the X-ray crystal structure of EaFAH, a dimeric fumarylacetoacetate hydrolase from Exiguobacterium antarcticum, was determined, and its functional properties were investigated using biochemical methods. EaFAH adopts a mixed β-sandwich roll fold with a highly flexible lid region (Val-Leu), and an Mg ion is bound at the active site by coordinating to the three carboxylate oxygen atoms of Glu, Glu, and Asp. The hydrolytic activity of EaFAH toward various substrates, including linalyl acetate was investigated using native polyacrylamide gel electrophoresis, activity staining, gel filtration, circular dichroism spectroscopy, fluorescence, and enzyme assays.

PubMed: 30630595
DOI: 10.1016/j.bbrc.2018.12.183

Experimental method

X-RAY DIFFRACTION (2.1 Å)