6iym | pdb_00006iym

Fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum

spinqualitylabelsall models 6iym, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iym is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-sandwich roll fold with a highly flexible lid region (Val(73)-Leu(94)), and an Mg(2+) ion is bound at the active site by coordinating to the three carboxylate oxygen atoms of Glu(124), Glu(126), and Asp(155). 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. Structural and functional analysis of a dimeric fumarylacetoacetate hydrolase (EaFAH) from psychrophilic Exiguobacterium antarcticum.,Yoo W, Lee CW, Kim BY, Huong Luu Le LT, Park SH, Kim HW, Shin SC, Kim KK, Lee JH, Kim TD Biochem Biophys Res Commun. 2019 Feb 12;509(3):773-778. doi:, 10.1016/j.bbrc.2018.12.183. Epub 2019 Jan 8. PMID:30630595 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA