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1dos

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[[Image:1dos.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE==
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|PDB= 1dos |SIZE=350|CAPTION= <scene name='initialview01'>1dos</scene>, resolution 1.67&Aring;
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<StructureSection load='1dos' size='340' side='right'caption='[[1dos]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1dos]] 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=1DOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOS FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span>
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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]] 1.67&#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=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=1dos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dos OCA], [https://pdbe.org/1dos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dos RCSB], [https://www.ebi.ac.uk/pdbsum/1dos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dos ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dos OCA], [http://www.ebi.ac.uk/pdbsum/1dos PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dos RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ALF_ECOLI ALF_ECOLI] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.<ref>PMID:10712619</ref>
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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/do/1dos_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=1dos ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
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==See Also==
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.
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__TOC__
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</StructureSection>
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==About this Structure==
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1DOS 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=1DOS OCA].
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==Reference==
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Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase., Blom NS, Tetreault S, Coulombe R, Sygusch J, Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8836102 8836102]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Fructose-bisphosphate aldolase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Blom N]]
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[[Category: Blom, N.]]
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[[Category: Coulombe R]]
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[[Category: Coulombe, R.]]
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[[Category: Sygusch J]]
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[[Category: Sygusch, J.]]
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[[Category: Tetreault S]]
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[[Category: Tetreault, S.]]
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[[Category: classii fructose 1,6-bisphosphate aldolase]]
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[[Category: glycolysis]]
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[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:42 2008''
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Current revision

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

PDB ID 1dos

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