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7a9j

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Crystal structure of the R395G mutant form of Coronafacic Acid Ligase from Pectobacterium brasiliense

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Categories: Large Structures | Pectobacterium brasiliense | Levy CW

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 <StructureSection load='7a9j' size='340' side='right'caption='[[7a9j]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7a9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"erwinia_carotovora_subsp._brasiliensis"_duarte_et_al._2004 "erwinia carotovora subsp. brasiliensis" duarte et al. 2004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A9J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7a9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_brasiliense Pectobacterium brasiliense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A9J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=R4Z:6-ethyl-1-oxidanylidene-indene-4-carboxylic+acid'>R4Z</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cfl, KCO_08370, KU74_07105 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=180957 "Erwinia carotovora subsp. brasiliensis" Duarte et al. 2004])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=R4Z:6-ethyl-1-oxidanylidene-indene-4-carboxylic+acid'>R4Z</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a9j OCA], [https://pdbe.org/7a9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a9j RCSB], [https://www.ebi.ac.uk/pdbsum/7a9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a9j ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/M4GWN4_9GAMM M4GWN4_9GAMM]
-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<ref>PMID:34012085</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7a9j" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Erwinia carotovora subsp. brasiliensis duarte et al. 2004]]
 [[Category: Large Structures]]
-[[Category: Levy, C W]]
+[[Category: Pectobacterium brasiliense]]
-[[Category: Ligase]]
+[[Category: Levy CW]]

7a9j

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Crystal structure of the R395G mutant form of Coronafacic Acid Ligase from Pectobacterium brasiliense

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