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1ofg

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(New page: 200px<br /><applet load="1ofg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ofg, resolution 2.7&Aring;" /> '''GLUCOSE-FRUCTOSE OXID...)
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[[Image:1ofg.gif|left|200px]]<br /><applet load="1ofg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ofg, resolution 2.7&Aring;" />
 
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'''GLUCOSE-FRUCTOSE OXIDOREDUCTASE'''<br />
 
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==Overview==
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==GLUCOSE-FRUCTOSE OXIDOREDUCTASE==
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BACKGROUND: The organism Zymomonas mobilis occurs naturally in sugar-rich, environments. To protect the bacterium against osmotic shock, the, periplasmic enzyme glucose-fructose oxidoreductase (GFOR) produces the, compatible, solute sorbitol by reduction of fructose, coupled with the, oxidation of glucose to gluconolactone. Hence, Z mobilis can tolerate high, concentrations of sugars and this property may be useful in the, development of an efficient microbial process for ethanol production. Each, enzyme subunit contains tightly associated NADP which is not released, during the catalytic cycle. RESULTS: The structure of GFOR was determined, by X-ray crystallography at 2.7 A resolution. Each subunit of the, tetrameric enzyme comprises two domains, a classical dinucleotide-binding, domain, and a C-terminal domain based on a predominantly antiparallel, nine-stranded beta sheet. In the tetramer, the subunits associate to form, two extended 18-stranded beta sheets, which pack against each other in a, face to face fashion, creating an extensive interface at the core of the, tetramer. An N-terminal arm from each subunit wraps around the, dinucleotide-binding domain of an adjacent subunit, covering the adenine, ring of NADP. CONCLUSIONS: In GFOR, the NADP is found associated with a, classical dinucleotide-binding domain in a conventional fashion. The NADP, is effectively buried in the protein-subunit interior as a result of, interactions with the N-terminal arm from an adjacent subunit in the, tetramer, and with a short helix from the C-terminal domain of the, protein. This accounts for NADP's inability to dissociate. The N-terminal, arm may also contribute to stabilization of the tetramer. The enzyme has, an unexpected structural similarity with the cytoplasmic enzyme, glucose-6-phosphate dehydrogenase (G6PD). We hypothesize that both enzymes, have diverged from a common ancestor. The mechanism of catalysis is still, unclear, but we have identified a conserved structural motif (Glu-Lys-Pro), in the active site of GFOR and G6PD that may be important for catalysis.
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<StructureSection load='1ofg' size='340' side='right'caption='[[1ofg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ofg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OFG FirstGlance]. <br>
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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]] 2.7&#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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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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=1ofg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ofg OCA], [https://pdbe.org/1ofg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ofg RCSB], [https://www.ebi.ac.uk/pdbsum/1ofg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ofg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GFO_ZYMMO GFO_ZYMMO]
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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/of/1ofg_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=1ofg ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1OFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with NDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose--fructose_oxidoreductase Glucose--fructose oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.28 1.1.99.28] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OFG OCA].
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*[[Glucose-fructose oxidoreductase|Glucose-fructose oxidoreductase]]
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__TOC__
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==Reference==
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</StructureSection>
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The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP., Kingston RL, Scopes RK, Baker EN, Structure. 1996 Dec 15;4(12):1413-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8994968 8994968]
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[[Category: Large Structures]]
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[[Category: Glucose--fructose oxidoreductase]]
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[[Category: Single protein]]
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[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
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[[Category: Baker, E.N.]]
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[[Category: Baker EN]]
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[[Category: Kingston, R.L.]]
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[[Category: Kingston RL]]
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[[Category: Scopes, R.K.]]
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[[Category: Scopes RK]]
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[[Category: NDP]]
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[[Category: nadp binding]]
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[[Category: osmotic protection]]
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[[Category: oxidoreductase]]
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[[Category: periplasm]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:56:30 2007''
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Current revision

GLUCOSE-FRUCTOSE OXIDOREDUCTASE

PDB ID 1ofg

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