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1q7b

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[[Image:1q7b.jpg|left|200px]]
 
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{{Structure
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==The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+==
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|PDB= 1q7b |SIZE=350|CAPTION= <scene name='initialview01'>1q7b</scene>, resolution 2.05&Aring;
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<StructureSection load='1q7b' size='340' side='right'caption='[[1q7b]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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<table><tr><td colspan='2'>[[1q7b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7B FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100]
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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]] 2.05&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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}}
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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=1q7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7b OCA], [https://pdbe.org/1q7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7b RCSB], [https://www.ebi.ac.uk/pdbsum/1q7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABG_ECOLI FABG_ECOLI] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.<ref>PMID:8631920</ref> <ref>PMID:14996818</ref>
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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/q7/1q7b_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=1q7b ConSurf].
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<div style="clear:both"></div>
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'''The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+'''
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==See Also==
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*[[Beta-ketoacyl carrier protein reductase 3D structures|Beta-ketoacyl carrier protein reductase 3D structures]]
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== References ==
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==Overview==
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<references/>
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beta-Ketoacyl-acyl carrier protein reductase (FabG) is a key component in the type II fatty acid synthase system. The structures of Escherichia coli FabG and the FabG[Y151F] mutant in binary complexes with NADP(H) reveal that mechanistically important conformational changes accompany cofactor binding. The active site Ser-Tyr-Lys triad is repositioned into a catalytically competent constellation, and a hydrogen bonded network consisting of ribose hydroxyls, the Ser-Tyr-Lys triad, and four water molecules creates a proton wire to replenish the tyrosine proton donated during catalysis. Also, a disordered loop in FabG forms a substructure in the complex that shapes the entrance to the active site. A key observation is that the nicotinamide portion of the cofactor is disordered in the FabG[Y151F].NADP(H) complex, and Tyr151 appears to be necessary for high-affinity cofactor binding. Biochemical data confirm that FabG[Y151F] is defective in NADPH binding. Finally, structural changes consistent with the observed negative cooperativity of FabG are described.
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__TOC__
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</StructureSection>
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==About this Structure==
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1Q7B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7B OCA].
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==Reference==
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Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG., Price AC, Zhang YM, Rock CO, White SW, Structure. 2004 Mar;12(3):417-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15016358 15016358]
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[[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Price, A C.]]
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[[Category: Price AC]]
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[[Category: Rock, C O.]]
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[[Category: Rock CO]]
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[[Category: White, S M.]]
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[[Category: White SM]]
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[[Category: Zhang, Y M.]]
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[[Category: Zhang Y-M]]
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[[Category: CA]]
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[[Category: NAP]]
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[[Category: oxoacyl reductase; nadp+; crystal structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:55 2008''
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Current revision

The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+

PDB ID 1q7b

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