7a9i | pdb_00007a9i

Crystal structure of Coronafacic Acid Ligase from Pectobacterium brasiliense

spinqualitylabelsall models 7a9i, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7a9i is a 1 chain structure with sequence from "erwinia_carotovora_subsp._brasiliensis"_duarte_et_al._2004 "erwinia carotovora subsp. brasiliensis" duarte et al. 2004. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4, R4Z Gene: cfl, KCO_08370, KU74_07105 ("Erwinia carotovora subsp. brasiliensis" Duarte et al. 2004) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Coronatine and related bacterial phytotoxins are mimics of the hormone jasmonyl-L-isoleucine (JA-Ile), which mediates physiologically important plant signalling pathways(1-4). Coronatine-like phytotoxins disrupt these essential pathways and have potential in the development of safer, more selective herbicides. Although the biosynthesis of coronatine has been investigated previously, the nature of the enzyme that catalyses the crucial coupling of coronafacic acid to amino acids remains unknown(1,2). Here we characterize a family of enzymes, coronafacic acid ligases (CfaLs), and resolve their structures. We found that CfaL can also produce JA-Ile, despite low similarity with the Jar1 enzyme that is responsible for ligation of JA and L-Ile in plants(5). This suggests that Jar1 and CfaL evolved independently to catalyse similar reactions-Jar1 producing a compound essential for plant development(4,5), and the bacterial ligases producing analogues toxic to plants. We further demonstrate how CfaL enzymes can be used to synthesize a diverse array of amides, obviating the need for protecting groups. Highly selective kinetic resolutions of racemic donor or acceptor substrates were achieved, affording homochiral products. We also used structure-guided mutagenesis to engineer improved CfaL variants. Together, these results show that CfaLs can deliver a wide range of amides for agrochemical, pharmaceutical and other applications. Discovery, characterization and engineering of ligases for amide synthesis.,Winn M, Rowlinson M, Wang F, Bering L, Francis D, Levy C, Micklefield J Nature. 2021 May;593(7859):391-398. doi: 10.1038/s41586-021-03447-w. Epub 2021, May 19. PMID:34012085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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