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| | <StructureSection load='5doz' size='340' side='right'caption='[[5doz]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='5doz' size='340' side='right'caption='[[5doz]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5doz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DOZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5doz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lyngbya_majuscula Lyngbya majuscula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DOZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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]] 2.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dov|5dov]], [[5dp1|5dp1]], [[5dp2|5dp2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5doz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5doz OCA], [http://pdbe.org/5doz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5doz RCSB], [http://www.ebi.ac.uk/pdbsum/5doz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5doz ProSAT]</span></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=5doz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5doz OCA], [https://pdbe.org/5doz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5doz RCSB], [https://www.ebi.ac.uk/pdbsum/5doz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5doz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6E7K0_9CYAN Q6E7K0_9CYAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Lyngbya majuscula]] | | [[Category: Lyngbya majuscula]] |
| - | [[Category: Khare, D]] | + | [[Category: Khare D]] |
| - | [[Category: Smith, J L]] | + | [[Category: Smith JL]] |
| - | [[Category: Cyclopropane]]
| + | |
| - | [[Category: Enoyl reductase]]
| + | |
| - | [[Category: Nadph]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Polyketide synthase]]
| + | |
| Structural highlights
Function
Q6E7K0_9CYAN
Publication Abstract from PubMed
The natural product curacin A, a potent anticancer agent, contains a rare cyclopropane group. The five enzymes for cyclopropane biosynthesis are highly similar to enzymes that generate a vinyl chloride moiety in the jamaicamide natural product. The structural biology of this remarkable catalytic adaptability is probed with high-resolution crystal structures of the curacin cyclopropanase (CurF ER), an in vitro enoyl reductase (JamJ ER), and a canonical curacin enoyl reductase (CurK ER). The JamJ and CurK ERs catalyze NADPH-dependent double bond reductions typical of enoyl reductases (ERs) of the medium-chain dehydrogenase reductase (MDR) superfamily. Cyclopropane formation by CurF ER is specified by a short loop which, when transplanted to JamJ ER, confers cyclopropanase activity on the chimeric enzyme. Detection of an adduct of NADPH with the model substrate crotonyl-CoA provides indirect support for a recent proposal of a C2-ene intermediate on the reaction pathway of MDR enoyl-thioester reductases.
Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase.,Khare D, Hale WA, Tripathi A, Gu L, Sherman DH, Gerwick WH, Hakansson K, Smith JL Structure. 2015 Oct 24. pii: S0969-2126(15)00405-0. doi:, 10.1016/j.str.2015.09.013. PMID:26526850[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Khare D, Hale WA, Tripathi A, Gu L, Sherman DH, Gerwick WH, Hakansson K, Smith JL. Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase. Structure. 2015 Oct 24. pii: S0969-2126(15)00405-0. doi:, 10.1016/j.str.2015.09.013. PMID:26526850 doi:http://dx.doi.org/10.1016/j.str.2015.09.013
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