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New page: left|200px<br /><applet load="1fpb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpb, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1fpb.jpg|left|200px]]<br /><applet load="1fpb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fpb, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION==
The three-dimensional structure of the complex between fructose, 1,6-bisphosphatase (EC 3.1.3.11) and the physiological inhibitor, beta-D-fructose 2,6-bisphosphate (Fru-2,6-P2), an analogue of the, substrate (fructose 1,6-bisphosphate), has been refined at 2.6-A, resolution to a residual error (R) factor of 0.171. The rms deviations are, 0.012 A and 2.88 degrees from ideal geometries of bond lengths and angles, respectively. The Fru-2,6-P2 occupies the active sites of both, polypeptides C1 and C2 in the crystallographic asymmetric unit in the, space group P3(2)21. The furanose and 6-phosphate of Fru-2,6-P2 are, located at the fructose 6-phosphate site established earlier, and the, 2-phosphate binds to the OH of Ser-124, the NH3+ of Lys-274, and the, backbone NH of Gly-122 and Ser-123. Backbone displacements of 1 A occur, for residues from Asp-121 to Asn-125. Model building of substrate, alpha-D-Fru-1,6-P2 based on the binding structure of Fru-2,6-P2 in the, active site shows interactions of the 1-phosphate with the backbone NH of, Ser-123 and Ser-124. In the AMP sites, density peaks attributed to, Fru-2,6-P2 are seen in C1 (and C4) but not in C2 (and C3). This minor, binding of Fru-2,6-P2 to AMP sites partially explains the synergistic, interaction between AMP and Fru-2,6-P2 and the protection of the AMP site, from acetylation in the presence of Fru-2,6-P2. In the synergistic, interaction between AMP and Fru-2,6-P2, inhibition of catalytic metal, binding by the presence of Fru-2,6-P2 at the active site, and propagation, of structural changes over some 28 A along beta-strand B3 from residues, 121 to 125 in the active site to Lys-112 and Tyr-113 in the AMP site, as, well as movement of helices across the interdimeric interfaces, may affect, AMP binding and the subsequent R-to-T transition. In addition, occupancy, of Fru-2,6-P2 at the AMP sites of C1 and C4 may favor binding of AMP to, the remaining unoccupied AMP sites and thus promote the accompanying, quaternary conformational changes.
<StructureSection load='1fpb' size='340' side='right'caption='[[1fpb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fpb]] 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=1FPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpb OCA], [https://pdbe.org/1fpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpb RCSB], [https://www.ebi.ac.uk/pdbsum/1fpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fpb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FPB 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 FDP as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FPB OCA].
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution., Liang JY, Huang S, Zhang Y, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2404-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1312721 1312721]
[[Category: Large Structures]]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Huang, S.]]
[[Category: Huang S]]
[[Category: Ke, H.]]
[[Category: Ke H]]
[[Category: Liang, J.Y.]]
[[Category: Liang JY]]
[[Category: Lipscomb, W.N.]]
[[Category: Lipscomb WN]]
[[Category: Zhang, Y.]]
[[Category: Zhang Y]]
[[Category: FDP]]
[[Category: hydrolase(phosphoric monoester)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:07:04 2007''

Latest revision as of 07:17, 7 February 2024

CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION

1fpb, resolution 2.60Å

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