1wdl

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[[Image:1wdl.gif|left|200px]]
 
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==fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form II (native4)==
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The line below this paragraph, containing "STRUCTURE_1wdl", creates the "Structure Box" on the page.
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<StructureSection load='1wdl' size='340' side='right'caption='[[1wdl]], [[Resolution|resolution]] 3.50&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'>[[1wdl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fragi Pseudomonas fragi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDL 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]] 3.5&#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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=N8E:3,6,9,12,15-PENTAOXATRICOSAN-1-OL'>N8E</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_1wdl| PDB=1wdl | 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=1wdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdl OCA], [https://pdbe.org/1wdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdl RCSB], [https://www.ebi.ac.uk/pdbsum/1wdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FADB_PSEFR FADB_PSEFR] Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.[HAMAP-Rule:MF_01621]
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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/wd/1wdl_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=1wdl ConSurf].
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<div style="clear:both"></div>
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'''fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form II (native4)'''
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==See Also==
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*[[Thiolase 3D structures|Thiolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The atomic view of the active site coupling termed channelling is a major subject in molecular biology. We have determined two distinct crystal structures of the bacterial multienzyme complex that catalyzes the last three sequential reactions in the fatty acid beta-oxidation cycle. The alpha2beta2 heterotetrameric structure shows the uneven ring architecture, where all the catalytic centers of 2-enoyl-CoA hydratase (ECH), L-3-hydroxyacyl-CoA dehydrogenase (HACD) and 3-ketoacyl-CoA thiolase (KACT) face a large inner solvent region. The substrate, anchored through the 3'-phosphate ADP moiety, allows the fatty acid tail to pivot from the ECH to HACD active sites, and finally to the KACT active site. Coupling with striking domain rearrangements, the incorporation of the tail into the KACT cavity and the relocation of 3'-phosphate ADP bring the reactive C2-C3 bond to the correct position for cleavage. The alpha-helical linker specific for the multienzyme contributes to the pivoting center formation and the substrate transfer through its deformation. This channelling mechanism could be applied to other beta-oxidation multienzymes, as revealed from the homology model of the human mitochondrial trifunctional enzyme complex.
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[[Category: Large Structures]]
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==About this Structure==
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1WDL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fragi Pseudomonas fragi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDL OCA].
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==Reference==
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Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex., Ishikawa M, Tsuchiya D, Oyama T, Tsunaka Y, Morikawa K, EMBO J. 2004 Jul 21;23(14):2745-54. Epub 2004 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15229654 15229654]
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[[Category: Acetyl-CoA C-acyltransferase]]
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[[Category: Protein complex]]
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[[Category: Pseudomonas fragi]]
[[Category: Pseudomonas fragi]]
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[[Category: Ishikawa, M.]]
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[[Category: Ishikawa M]]
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[[Category: Morikawa, K.]]
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[[Category: Morikawa K]]
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[[Category: Oyama, T.]]
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[[Category: Oyama T]]
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[[Category: Tsuchiya, D.]]
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[[Category: Tsuchiya D]]
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[[Category: Tsunaka, Y.]]
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[[Category: Tsunaka Y]]
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[[Category: Alpha2beta2 heterotetrameric complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:30:32 2008''
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Current revision

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form II (native4)

PDB ID 1wdl

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