1ps9

<table><tr><td colspan='2'>[[1ps9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PS9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MDE:5-MERCAPTOETHANOL-2-DECENOYL-COENZYME+A'>MDE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,4-dienoyl-CoA_reductase_(NADPH) 2,4-dienoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.34 1.3.1.34] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ps9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps9 OCA], [http://pdbe.org/1ps9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ps9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ps9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ps9 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FADH_ECOLI FADH_ECOLI]] Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-2- enoyl-CoA.

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== Publication Abstract from PubMed ==

Escherichia coli 2,4-dienoyl-CoA reductase is an iron-sulfur flavoenzyme required for the metabolism of unsaturated fatty acids with double bonds at even carbon positions. The enzyme contains FMN, FAD, and a 4Fe-4S cluster and exhibits sequence homology to another iron-sulfur flavoprotein, trimethylamine dehydrogenase. It also requires NADPH as an electron source, resulting in reduction of the C4-C5 double bond of the acyl chain of the CoA thioester substrate. The structure presented here of a ternary complex of E. coli 2,4-dienoyl-CoA reductase with NADP+ and a fatty acyl-CoA substrate reveals a possible mechanism for substrate reduction and provides details of a plausible electron transfer mechanism involving both flavins and the iron-sulfur cluster. The reaction is initiated by hydride transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. In the final stages of the reaction, the fully reduced FMN provides a hydride ion to the C5 atom of substrate, and Tyr-166 and His-252 are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and complete the reaction. Inspection of the substrate binding pocket explains the relative promiscuity of the enzyme, catalyzing reduction of both 2-trans,4-cis- and 2-trans,4-trans-dienoyl-CoA thioesters.

The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase.,Hubbard PA, Liang X, Schulz H, Kim JJ J Biol Chem. 2003 Sep 26;278(39):37553-60. Epub 2003 Jul 2. PMID:12840019<ref>PMID:12840019</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ps9" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Hubbard, P A]]

[[Category: Kim, J J]]

[[Category: Liang, X]]

[[Category: Schulz, H]]

[[Category: Tim barrel]]