1rdz

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(New page: 200px<br /><applet load="1rdz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rdz, resolution 2.05&Aring;" /> '''T-STATE STRUCTURE OF...)
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[[Image:1rdz.jpg|left|200px]]<br /><applet load="1rdz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rdz, resolution 2.05&Aring;" />
 
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'''T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI'''<br />
 
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==Overview==
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==T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI==
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The active site of pig kidney fructose-1,6-bisphosphatase (EC 3.1.3.11) is, shared between subunits, Arg-243 of one chain interacting with, fructose-1,6-bisphosphate or fructose-2,6-bisphosphate in the active site, of an adjacent chain. In this study, we present the X-ray structures of, the mutant version of the enzyme with Arg-243 replaced by alanine, crystallized in both T and R allosteric states. Kinetic characteristics of, the altered enzyme showed the magnesium binding and inhibition by AMP, differed slightly; affinity for the substrate fructose-1,6-bisphosphate, was reduced 10-fold and affinity for the inhibitor, fructose-2,6-bisphosphate was reduced 1,000-fold (Giroux E, Williams MK, Kantrowitz ER, 1994, J Biol Chem 269:31404-31409). The X-ray structures, show no major changes in the organization of the active site compared with, wild-type enzyme, and the structures confirm predictions of molecular, dynamics simulations involving Lys-269 and Lys-274. Comparison of two, independent models of the T form structures have revealed small but, significant changes in the conformation of the bound AMP molecules and, small reorganization of the active site correlated with the presence of, the inhibitor. The differences in kinetic properties of the mutant enzyme, indicate the key importance of Arg-243 in the function of, fructose-1,6-bisphosphatase. Calculations using the X-ray structures of, the Arg-243--&gt;Ala enzyme suggest that the role of Arg-243 in the wild-type, enzyme is predominantly electrostatic in nature.
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<StructureSection load='1rdz' size='340' side='right'caption='[[1rdz]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rdz]] 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=1RDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RDZ FirstGlance]. <br>
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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]] 2.05&#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>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
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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=1rdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rdz OCA], [https://pdbe.org/1rdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rdz RCSB], [https://www.ebi.ac.uk/pdbsum/1rdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rdz 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/rd/1rdz_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=1rdz ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1RDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with F6P and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RDZ OCA].
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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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==Reference==
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</StructureSection>
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Crystal structures of the active site mutant (Arg-243--&gt;Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli., Stec B, Abraham R, Giroux E, Kantrowitz ER, Protein Sci. 1996 Aug;5(8):1541-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8844845 8844845]
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[[Category: Large Structures]]
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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: Abraham, R.]]
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[[Category: Abraham R]]
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[[Category: Giroux, E.]]
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[[Category: Giroux E]]
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[[Category: Kantrowitz, E.R.]]
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[[Category: Kantrowitz ER]]
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[[Category: Stec, B.]]
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[[Category: Stec B]]
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[[Category: AMP]]
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[[Category: F6P]]
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[[Category: hydrolase r243a mutant in the t-state]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:30:40 2007''
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Current revision

T-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI

PDB ID 1rdz

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