1h6c: Difference between revisions
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== | ==Oxidized Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with succinate== | ||
<StructureSection load='1h6c' size='340' side='right'caption='[[1h6c]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1h6c]] is a 2 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=1H6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H6C FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6c OCA], [https://pdbe.org/1h6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h6c RCSB], [https://www.ebi.ac.uk/pdbsum/1h6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h6c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GFO_ZYMMO GFO_ZYMMO] | |||
== 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/h6/1h6c_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=1h6c ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The NADP(H)-dependent enzyme glucose-fructose oxidoreductase (GFOR) is a classic example of a redox protein that is translocated across a membrane in fully folded form. GFOR is synthesized in the cytoplasm with a 52-residue signal peptide, giving a precursor form, preGFOR, that is fully active and has its cofactor tightly bound. A twin-arginine motif in the signal peptide directs it to a Sec-independent pathway by which it is translocated, in fully folded form, into the periplasm where it functions to produce sorbitol for osmoprotection. We have determined the crystal structures of four different forms of preGFOR, (i) oxidized preGFOR, with succinate bound in the active site, (ii) oxidized preGFOR with glycerol bound, (iii) reduced preGFOR in 0.3 M glucose, and (iv) reduced preGFOR in 1.5 M sorbitol, at resolutions of 2.2, 2.05, 2.5, and 2.6 A, respectively. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus; a factor contributing to this disorder may be the high positive charge of the protein surface in the region where the signal peptide emerges. This may disfavor a stable association between the signal peptide and the rest of the protein. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding, explaining the enzymatic activity of the precursor form. In the glycerol complex, preGFOR(gll), a bound glycerol molecule models the binding of the glucose substrate, with its O1 atom hydrogen bonded to the essential acid/base catalyst, Tyr269, and C1 only 3 A from C4 of the nicotinamide. In the glucose-soaked structure, preGFOR(glu), we identify a conformational change of the nearby Lys181 that probably results from the oxidation of glucose to gluconolactone, and functions to prevent rebinding of glucose prior to the binding of fructose. In this conformational change, the Lys181 side chain moves closer to the nicotinamide ring, stabilized by its increased negative charge. | The NADP(H)-dependent enzyme glucose-fructose oxidoreductase (GFOR) is a classic example of a redox protein that is translocated across a membrane in fully folded form. GFOR is synthesized in the cytoplasm with a 52-residue signal peptide, giving a precursor form, preGFOR, that is fully active and has its cofactor tightly bound. A twin-arginine motif in the signal peptide directs it to a Sec-independent pathway by which it is translocated, in fully folded form, into the periplasm where it functions to produce sorbitol for osmoprotection. We have determined the crystal structures of four different forms of preGFOR, (i) oxidized preGFOR, with succinate bound in the active site, (ii) oxidized preGFOR with glycerol bound, (iii) reduced preGFOR in 0.3 M glucose, and (iv) reduced preGFOR in 1.5 M sorbitol, at resolutions of 2.2, 2.05, 2.5, and 2.6 A, respectively. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus; a factor contributing to this disorder may be the high positive charge of the protein surface in the region where the signal peptide emerges. This may disfavor a stable association between the signal peptide and the rest of the protein. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding, explaining the enzymatic activity of the precursor form. In the glycerol complex, preGFOR(gll), a bound glycerol molecule models the binding of the glucose substrate, with its O1 atom hydrogen bonded to the essential acid/base catalyst, Tyr269, and C1 only 3 A from C4 of the nicotinamide. In the glucose-soaked structure, preGFOR(glu), we identify a conformational change of the nearby Lys181 that probably results from the oxidation of glucose to gluconolactone, and functions to prevent rebinding of glucose prior to the binding of fructose. In this conformational change, the Lys181 side chain moves closer to the nicotinamide ring, stabilized by its increased negative charge. | ||
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.,Nurizzo D, Halbig D, Sprenger GA, Baker EN Biochemistry. 2001 Nov 20;40(46):13857-67. PMID:11705375<ref>PMID:11705375</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 1h6c" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[Glucose-fructose oxidoreductase|Glucose-fructose oxidoreductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Zymomonas mobilis]] | [[Category: Zymomonas mobilis]] | ||
[[Category: Baker | [[Category: Baker EN]] | ||
[[Category: Nurizzo | [[Category: Nurizzo D]] | ||
Latest revision as of 15:18, 13 December 2023
Oxidized Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with succinateOxidized Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with succinate
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe NADP(H)-dependent enzyme glucose-fructose oxidoreductase (GFOR) is a classic example of a redox protein that is translocated across a membrane in fully folded form. GFOR is synthesized in the cytoplasm with a 52-residue signal peptide, giving a precursor form, preGFOR, that is fully active and has its cofactor tightly bound. A twin-arginine motif in the signal peptide directs it to a Sec-independent pathway by which it is translocated, in fully folded form, into the periplasm where it functions to produce sorbitol for osmoprotection. We have determined the crystal structures of four different forms of preGFOR, (i) oxidized preGFOR, with succinate bound in the active site, (ii) oxidized preGFOR with glycerol bound, (iii) reduced preGFOR in 0.3 M glucose, and (iv) reduced preGFOR in 1.5 M sorbitol, at resolutions of 2.2, 2.05, 2.5, and 2.6 A, respectively. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus; a factor contributing to this disorder may be the high positive charge of the protein surface in the region where the signal peptide emerges. This may disfavor a stable association between the signal peptide and the rest of the protein. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding, explaining the enzymatic activity of the precursor form. In the glycerol complex, preGFOR(gll), a bound glycerol molecule models the binding of the glucose substrate, with its O1 atom hydrogen bonded to the essential acid/base catalyst, Tyr269, and C1 only 3 A from C4 of the nicotinamide. In the glucose-soaked structure, preGFOR(glu), we identify a conformational change of the nearby Lys181 that probably results from the oxidation of glucose to gluconolactone, and functions to prevent rebinding of glucose prior to the binding of fructose. In this conformational change, the Lys181 side chain moves closer to the nicotinamide ring, stabilized by its increased negative charge. Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.,Nurizzo D, Halbig D, Sprenger GA, Baker EN Biochemistry. 2001 Nov 20;40(46):13857-67. PMID:11705375[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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