5dp2: Difference between revisions

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'''Unreleased structure'''


The entry 5dp2 is ON HOLD  until Paper Publication
==CurF ER cyclopropanase from curacin A biosynthetic pathway==
<StructureSection load='5dp2' size='340' side='right'caption='[[5dp2]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dp2]] is a 1 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=5DP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DP2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.96&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5dp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dp2 OCA], [https://pdbe.org/5dp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dp2 RCSB], [https://www.ebi.ac.uk/pdbsum/5dp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dp2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6DNE7_9CYAN Q6DNE7_9CYAN]
<div style="background-color:#fffaf0;">
== 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.


Authors: Khare, D., Smith, J.L.
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<ref>PMID:26526850</ref>


Description: CurF ER cyclopropanase from curacin A biosynthetic pathway
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Smith, J.L]]
<div class="pdbe-citations 5dp2" style="background-color:#fffaf0;"></div>
[[Category: Khare, D]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lyngbya majuscula]]
[[Category: Khare D]]
[[Category: Smith JL]]
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