4fbp

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[[Image:4fbp.jpg|left|200px]]
 
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==CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)==
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The line below this paragraph, containing "STRUCTURE_4fbp", creates the "Structure Box" on the page.
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<StructureSection load='4fbp' size='340' side='right'caption='[[4fbp]], [[Resolution|resolution]] 2.50&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'>[[4fbp]] is a 4 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=4FBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FBP 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]] 2.5&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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{{STRUCTURE_4fbp| PDB=4fbp | 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=4fbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fbp OCA], [https://pdbe.org/4fbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fbp RCSB], [https://www.ebi.ac.uk/pdbsum/4fbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fbp 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/fb/4fbp_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=4fbp ConSurf].
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<div style="clear:both"></div>
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'''CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)'''
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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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A structure of the neutral form of fructose-1,6-bisphosphatase complexed with AMP has been determined by the molecular replacement method and refined at a 2.5-A resolution to a crystallographic R factor of 0.169. The root-mean-square errors of the structure from standard geometry are 0.013 A for bond lengths and 2.99 degrees for bond angles. Comparison of the AMP complex with the F6P complex shows that dimer C3-C4 twists about 19 degrees about a molecular 2-fold axis when dimers C1-C2 of the R and T forms of the enzyme are superimposed one another and that a slight shift of about 1 A of the AMP domain partially compensates this twist. The R to T transition of the enzyme does not significantly change the conformation of the F6P-binding site. However, residues at the divalent metal site and the AMP site show significant positional shifts. If these results can be extended to substrate in place of F6P, they suggest that regulation of the enzyme by AMP may occur partly through effects on metal-ion affinity or position. AMP binds to the same sites of the T and R forms, but only half-occupancy was observed in the alkaline R form. Sequential binding of AMP, at least in pairs, is suggested as the unligated R form is converted to the T form. Two possible pathways are suggested for allosteric communication over about 28 A between the AMP site and the active site: one via helices H1, H2, and H3 and another via the eight-stranded beta-sheet.(ABSTRACT TRUNCATED AT 250 WORDS)
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[[Category: Large Structures]]
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==About this Structure==
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4FBP 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=4FBP OCA].
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==Reference==
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Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form)., Ke HM, Liang JY, Zhang YP, Lipscomb WN, Biochemistry. 1991 May 7;30(18):4412-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1850623 1850623]
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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: Ke, H.]]
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[[Category: Ke H]]
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[[Category: Liang, J Y.]]
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[[Category: Liang J-Y]]
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[[Category: Lipscomb, W N.]]
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[[Category: Lipscomb WN]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:48 2008''
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Current revision

CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)

PDB ID 4fbp

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