1spi

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(New page: 200px<br /><applet load="1spi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1spi, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1spi.gif|left|200px]]<br /><applet load="1spi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1spi, resolution 2.8&Aring;" />
 
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'''CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION==
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The three-dimensional structure of the spinach chloroplast, fructose-1,6-bisphosphatase (Fru-1,6-Pase) has been solved by the, molecular replacement method at 2.8 A resolution and refined to a, crystallographic R factor of 0.203. The enzyme is composed of four, monomers and displays pseudo D2 symmetry. Comparison with the allosteric, Fru-1,6-Pase from pig kidney shows orientationally displaced dimers within, the quaternary structure of the chloroplast enzyme. When the C1C2 dimers, of the two enzymes are superimposed, the C3C4 dimer of the chloroplast, enzyme is rotated 20 degrees and 5 degrees relative to the C3C4 dimer of, the R and T forms of the pig kidney enzyme, respectively. This new, quaternary structure, designated as S, may be described as a super-T form, and is outside of the pathway of the allosteric transition which occurs in, the pig kidney enzyme, which shows a 15 degrees rotation between T and R, forms. Chloroplast Fru-1,6-Pase, unlike the pig kidney enzyme, is, insensitive to allosteric transformation by AMP. Structural changes in the, AMP binding site involving mainly helices H1, H2, and H3 and the loop, between H1 and H2 at the dimer interface interfere with binding of the, phosphate of AMP. Finally, the location of cysteines residues provides a, basis for a preliminary discussion of the activation of the enzyme by, reduction of cysteines via the ferredoxin-thioredoxin f system; this, process is complementary to activation by pH changes, Mg2+ or Ca2+, Fru-1,6-P2, and possibly Fru-2,6-P2.
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<StructureSection load='1spi' size='340' side='right'caption='[[1spi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1spi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPI 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]] 2.8&#8491;</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=1spi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spi OCA], [https://pdbe.org/1spi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1spi RCSB], [https://www.ebi.ac.uk/pdbsum/1spi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1spi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F16P1_SPIOL F16P1_SPIOL]
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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/sp/1spi_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=1spi 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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1SPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. 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=1SPI 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 structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 A resolution., Villeret V, Huang S, Zhang Y, Xue Y, Lipscomb WN, Biochemistry. 1995 Apr 4;34(13):4299-306. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7703243 7703243]
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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: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
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[[Category: Huang, S.]]
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[[Category: Huang S]]
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[[Category: Lipscomb, W.N.]]
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[[Category: Lipscomb WN]]
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[[Category: Villeret, V.]]
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[[Category: Villeret V]]
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[[Category: Xue, Y.]]
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[[Category: Xue Y]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: hydrolase (phosphoric monoester)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:32:54 2007''
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Current revision

CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION

PDB ID 1spi

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