1nux

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{{Seed}}
 
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[[Image:1nux.png|left|200px]]
 
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==Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and inhibitory concentrations of Potassium (200mM)==
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The line below this paragraph, containing "STRUCTURE_1nux", creates the "Structure Box" on the page.
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<StructureSection load='1nux' size='340' side='right'caption='[[1nux]], [[Resolution|resolution]] 1.60&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'>[[1nux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NUX 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]] 1.6&#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=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene></td></tr>
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{{STRUCTURE_1nux| PDB=1nux | 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=1nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nux OCA], [https://pdbe.org/1nux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nux RCSB], [https://www.ebi.ac.uk/pdbsum/1nux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nux ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]
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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/nu/1nux_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=1nux ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The hydrolysis of a phosphate ester can proceed through an intermediate of metaphosphate (dissociative mechanism) or through a trigonal bipryamidal transition state (associative mechanism). Model systems in solution support the dissociative pathway, whereas most enzymologists favor an associative mechanism for enzyme-catalyzed reactions. Crystals of fructose-1,6-bisphosphatase grow from an equilibrium mixture of substrates and products at near atomic resolution (1.3 A). At neutral pH, products of the reaction (orthophosphate and fructose 6-phosphate) bind to the active site in a manner consistent with an associative reaction pathway; however, in the presence of inhibitory concentrations of K+ (200 mm), or at pH 9.6, metaphosphate and water (or OH-) are in equilibrium with orthophosphate. Furthermore, one of the magnesium cations in the pH 9.6 complex resides in an alternative position, and suggests the possibility of metal cation migration as the 1-phosphoryl group of the substrate undergoes hydrolysis. To the best of our knowledge, the crystal structures reported here represent the first direct observation of metaphosphate in a condensed phase and may provide the structural basis for fundamental changes in the catalytic mechanism of fructose-1,6-bisphosphatase in response to pH and different metal cation activators.
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===Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and inhibitory concentrations of Potassium (200mM)===
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Metaphosphate in the active site of fructose-1,6-bisphosphatase.,Choe JY, Iancu CV, Fromm HJ, Honzatko RB J Biol Chem. 2003 May 2;278(18):16015-20. Epub 2003 Feb 20. PMID:12595528<ref>PMID:12595528</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1nux" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12595528}}, adds the Publication Abstract to the page
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12595528 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12595528}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1NUX is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUX OCA].
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==Reference==
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<ref group="xtra">PMID:12595528</ref><references group="xtra"/>
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[[Category: Fructose-bisphosphatase]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Choe, J.]]
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[[Category: Choe J]]
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[[Category: Fromm, H J.]]
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[[Category: Fromm HJ]]
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[[Category: Honzatko, R B.]]
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[[Category: Honzatko RB]]
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[[Category: Iancu, C V.]]
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[[Category: Iancu CV]]
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[[Category: Allosteric enzyme]]
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[[Category: Bisphosphatase]]
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[[Category: Gluconeogenesis]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:59:58 2009''
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Current revision

Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and inhibitory concentrations of Potassium (200mM)

PDB ID 1nux

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