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[[Image:1q7c.jpg|left|200px]]


{{Structure
==The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment==
|PDB= 1q7c |SIZE=350|CAPTION= <scene name='initialview01'>1q7c</scene>, resolution 2.50&Aring;
<StructureSection load='1q7c' size='340' side='right'caption='[[1q7c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>
<table><tr><td colspan='2'>[[1q7c]] is a 2 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=1Q7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7C FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7c OCA], [https://pdbe.org/1q7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7c RCSB], [https://www.ebi.ac.uk/pdbsum/1q7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7c ProSAT]</span></td></tr>
|RELATEDENTRY=[[1q7b|1Q7B]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7c OCA], [http://www.ebi.ac.uk/pdbsum/1q7c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q7c RCSB]</span>
== Function ==
}}
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q7/1q7c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1q7c ConSurf].
<div style="clear:both"></div>


'''The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment'''
==See Also==
 
*[[Beta-ketoacyl carrier protein reductase 3D structures|Beta-ketoacyl carrier protein reductase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1Q7C 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=1Q7C OCA].
 
==Reference==
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]
[[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Price, A C.]]
[[Category: Price AC]]
[[Category: Rock, C O.]]
[[Category: Rock CO]]
[[Category: White, S M.]]
[[Category: White SM]]
[[Category: Zhang, Y M.]]
[[Category: Zhang Y-M]]
[[Category: crystal structure]]
[[Category: nadp+]]
[[Category: oxoacyl reductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:49 2008''

Latest revision as of 09:00, 21 February 2024

The structure of betaketoacyl-[ACP] reductase Y151F mutant in complex with NADPH fragment

1q7c, resolution 2.50Å

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