1edo

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[[Image:1edo.gif|left|200px]]
 
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{{Structure
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==THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+==
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|PDB= 1edo |SIZE=350|CAPTION= <scene name='initialview01'>1edo</scene>, resolution 2.3&Aring;
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<StructureSection load='1edo' size='340' side='right'caption='[[1edo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>
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<table><tr><td colspan='2'>[[1edo]] 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=1EDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDO FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.3&#8491;</td></tr>
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|GENE= OIL SEED RAPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3708 Brassica napus])
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<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>
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|DOMAIN=
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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=1edo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edo OCA], [https://pdbe.org/1edo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edo RCSB], [https://www.ebi.ac.uk/pdbsum/1edo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edo ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edo OCA], [http://www.ebi.ac.uk/pdbsum/1edo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1edo RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/FABG1_BRANA FABG1_BRANA]
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== Evolutionary Conservation ==
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'''THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edo_consurf.spt"</scriptWhenChecked>
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BACKGROUND: beta-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. RESULTS: The first crystal structure of BKR has been determined at 2.3 A resolution in a binary complex with an NADP(+) cofactor. The structure reveals a homotetramer in which each subunit has a classical dinucleotide-binding fold. A triad of Ser154, Tyr167 and Lys171 residues is found at the active site, characteristic of the SDR family. Overall BKR has a very similar structure to ENR with good superimposition of catalytically important groups. Modelling of the substrate into the active site of BKR indicates the need for conformational changes in the enzyme. CONCLUSIONS: A catalytic mechanism can be proposed involving the conserved triad. Helix alpha6 must shift its position to permit substrate binding to BKR and might act as a flexible lid on the active site. The similarities in fold, mechanism and substrate binding between BKR, which catalyzes a carbon-oxygen double-bond reduction, and ENR, the carbon-carbon double-bond oxidoreductase in FAS, suggest a close evolutionary link during the development of the fatty acid biosynthetic pathway.
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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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==About this Structure==
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</jmolCheckbox>
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1EDO 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=1EDO OCA].
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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=1edo ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis., Fisher M, Kroon JT, Martindale W, Stuitje AR, Slabas AR, Rafferty JB, Structure. 2000 Apr 15;8(4):339-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10801480 10801480]
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</StructureSection>
[[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: Fisher, M.]]
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[[Category: Fisher M]]
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[[Category: Kroon, J T.]]
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[[Category: Kroon JT]]
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[[Category: Martindale, W.]]
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[[Category: Martindale W]]
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[[Category: Rafferty, J B.]]
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[[Category: Rafferty JB]]
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[[Category: Slabas, A R.]]
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[[Category: Slabas AR]]
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[[Category: Stuitje, A R.]]
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[[Category: Stuitje AR]]
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[[Category: nucleotide fold]]
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[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:28 2008''
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Current revision

THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+

PDB ID 1edo

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