5zm2 | pdb_00005zm2

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AndA

spinqualitylabelsall models 5zm2, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zm2 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed AndA, an Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzyme, is the key enzyme that constructs the unique and congested bridged-ring system of anditomin (1), by catalyzing consecutive dehydrogenation and isomerization reactions. Although we previously characterized AndA to some extent, the means by which the enzyme facilitates this drastic structural reconstruction have remained elusive. In this study, we have solved three X-ray crystal structures of AndA, in its apo form and in the complexes with Fe(II), alphaKG, and two substrates. The crystal structures and mutational experiments identified several key amino acid residues important for the catalysis and provided insight into how AndA controls the reaction. Furthermore, computational calculations validated the proposed reaction mechanism for the bridged-ring formation and also revealed the requirement of a series of conformational changes during the transformation. Structural and Computational Bases for Dramatic Skeletal Rearrangement in Anditomin Biosynthesis.,Nakashima Y, Mitsuhashi T, Matsuda Y, Senda M, Sato H, Yamazaki M, Uchiyama M, Senda T, Abe I J Am Chem Soc. 2018 Jul 4. doi: 10.1021/jacs.8b06084. PMID:29972643 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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