1eyk

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[[Image:1eyk.jpg|left|200px]]
 
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{{Structure
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==FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)==
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|PDB= 1eyk |SIZE=350|CAPTION= <scene name='initialview01'>1eyk</scene>, resolution 2.23&Aring;
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<StructureSection load='1eyk' size='340' side='right'caption='[[1eyk]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
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<table><tr><td colspan='2'>[[1eyk]] is a 2 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=1EYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYK FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]
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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]] 2.23&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1eyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyk OCA], [https://pdbe.org/1eyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyk RCSB], [https://www.ebi.ac.uk/pdbsum/1eyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyk 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/ey/1eyk_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=1eyk ConSurf].
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<div style="clear:both"></div>
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'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)'''
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==See Also==
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.
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[[Category: Large Structures]]
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==About this Structure==
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1EYK is a [[Single protein]] 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=1EYK OCA].
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==Reference==
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Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes., Choe JY, Fromm HJ, Honzatko RB, Biochemistry. 2000 Jul 25;39(29):8565-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10913263 10913263]
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[[Category: Fructose-bisphosphatase]]
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[[Category: Single protein]]
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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: Honzatko, R B.]]
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[[Category: Honzatko RB]]
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[[Category: AMP]]
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[[Category: F6P]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: allosteric enzyme]]
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[[Category: bisphosphatase]]
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[[Category: gluconeogenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:59 2008''
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Current revision

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)

PDB ID 1eyk

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