1enp

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[[Image:1enp.jpg|left|200px]]
 
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==BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE==
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The line below this paragraph, containing "STRUCTURE_1enp", creates the "Structure Box" on the page.
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<StructureSection load='1enp' size='340' side='right'caption='[[1enp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1enp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ENP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_1enp| PDB=1enp | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1enp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enp OCA], [https://pdbe.org/1enp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1enp RCSB], [https://www.ebi.ac.uk/pdbsum/1enp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1enp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABI_BRANA FABI_BRANA] Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/en/1enp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1enp ConSurf].
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<div style="clear:both"></div>
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'''BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE'''
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==See Also==
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*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Enoyl acyl carrier protein reductase (ENR) catalyzes the NAD(P)H-dependent reduction of trans-delta 2-enoyl acyl carrier protein, an essential step in de novo fatty acid biosynthesis. Plants contain both NADH-dependent and separate NADPH-dependent ENR enzymes which form part of the dissociable type II fatty acid synthetase. Highly elevated levels of the NADH-dependent enzyme are found during lipid deposition in maturing seeds of oilseed rape (Brassica napus). RESULTS: The crystal structure of an ENR-NAD binary complex has been determined at 1.9 A resolution and consists of a homotetramer in which each subunit forms a single domain comprising a seven-stranded parallel beta sheet flanked by seven alpha helices. The subunit has a topology highly reminiscent of a dinucleotide-binding fold. The active site has been located by difference Fourier analysis of data from crystals equilibrated in NADH. CONCLUSIONS: The structure of ENR shows a striking similarity with the epimerases and short-chain alcohol dehydrogenases, in particular, 3 alpha,20 beta-hydroxysteroid dehydrogenase (HSD). The similarity with HSD extends to the conservation of a catalytically important lysine that stabilizes the transition state and to the use of a tyrosine as a base--with subtle modifications arising from differing requirements of the reduction chemistry.
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==About this Structure==
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1ENP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENP OCA].
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==Reference==
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Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase., Rafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW, Structure. 1995 Sep 15;3(9):927-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535786 8535786]
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[[Category: Brassica napus]]
[[Category: Brassica napus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Rafferty, J B.]]
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[[Category: Rafferty JB]]
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[[Category: Rice, D W.]]
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[[Category: Rice DW]]
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[[Category: Oxidoreductase]]
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[[Category: Plant lipid biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:19:08 2008''
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Current revision

BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE

PDB ID 1enp

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