5BK9
AAD-1 Bound to the Vanadyl Ion and Succinate
Summary for 5BK9
| Entry DOI | 10.2210/pdb5bk9/pdb |
| Descriptor | (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase, SUCCINIC ACID, oxovanadium(2+), ... (5 entities in total) |
| Functional Keywords | aryloxyalkanoate dioxygenase, herbicide degradation, biosynthetic protein, oxidoreductase |
| Biological source | Delftia acidovorans (Pseudomonas acidovorans) |
| Total number of polymer chains | 2 |
| Total formula weight | 66947.07 |
| Authors | Ongpipattanakul, C.,Chekan, J.R. (deposition date: 2019-06-01, release date: 2019-06-12, Last modification date: 2023-09-27) |
| Primary citation | Chekan, J.R.,Ongpipattanakul, C.,Wright, T.R.,Zhang, B.,Bollinger Jr., J.M.,Rajakovich, L.J.,Krebs, C.,Cicchillo, R.M.,Nair, S.K. Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants. Proc.Natl.Acad.Sci.USA, 116:13299-13304, 2019 Cited by PubMed Abstract: The synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) is an active ingredient of thousands of commercial herbicides. Multiple species of bacteria degrade 2,4-D via a pathway initiated by the Fe(II) and α-ketoglutarate (Fe/αKG)-dependent aryloxyalkanoate dioxygenases (AADs). Recently, genes encoding 2 AADs have been deployed commercially in herbicide-tolerant crops. Some AADs can also inactivate chiral phenoxypropionate and aryloxyphenoxypropionate (AOPP) herbicides, albeit with varying substrate enantioselectivities. Certain AAD enzymes, such as AAD-1, have expanded utility in weed control systems by enabling the use of diverse modes of action with a single trait. Here, we report 1) the use of a genomic context-based approach to identify 59 additional members of the AAD class, 2) the biochemical characterization of AAD-2 from USDA 110 as a catalyst to degrade ()-stereoisomers of chiral synthetic auxins and AOPP herbicides, 3) spectroscopic data that demonstrate the canonical ferryl complex in the AAD-1 reaction, and 4) crystal structures of representatives of the AAD class. Structures of AAD-1, an ()-enantiomer substrate-specific enzyme, in complexes with a phenoxypropionate synthetic auxin or with AOPP herbicides and of AAD-2, which has the opposite ()-enantiomeric substrate specificity, reveal the structural basis for stereoselectivity and provide insights into a common catalytic mechanism. PubMed: 31209034DOI: 10.1073/pnas.1900711116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
Download full validation report
