5ZM4
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AndA with preandiloid C
Summary for 5ZM4
| Entry DOI | 10.2210/pdb5zm4/pdb |
| Descriptor | Dioxygenase andA, FE (III) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total) |
| Functional Keywords | oxygenase, oxidoreductase |
| Biological source | Emericella variicolor (Aspergillus variecolor,Aspergillus stellatus) |
| Total number of polymer chains | 4 |
| Total formula weight | 137867.39 |
| Authors | Nakashima, Y.,Senda, T. (deposition date: 2018-04-01, release date: 2018-07-18, Last modification date: 2023-11-22) |
| Primary citation | Nakashima, Y.,Mitsuhashi, T.,Matsuda, Y.,Senda, M.,Sato, H.,Yamazaki, M.,Uchiyama, M.,Senda, T.,Abe, I. Structural and Computational Bases for Dramatic Skeletal Rearrangement in Anditomin Biosynthesis. J. Am. Chem. Soc., 140:9743-9750, 2018 Cited by PubMed Abstract: AndA, an Fe(II)/α-ketoglutarate (αKG)-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), αKG, 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. PubMed: 29972643DOI: 10.1021/jacs.8b06084 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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