1bk4

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(New page: 200px<br /><applet load="1bk4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bk4, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1bk4.gif|left|200px]]<br /><applet load="1bk4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bk4, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION==
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The three-dimensional structure of the R form of rabbit liver fructose, 1,6-bisphosphatase (Fru-1,6-Pase; E.C. 3.1.3.11) has been determined by a, combination of heavy-atom and molecular-replacement methods. A model, which includes 2394 protein atoms and 86 water molecules, has been refined, at 2.3 A resolution to a crystallographic R factor of 0.177. The, root-mean-square deviations of bond distances and angles from standard, geometry are 0.012 A and 1.7 degrees, respectively. This structural, result, in conjunction with recently redetermined amino-acid sequence, data, unequivocally establishes that the rabbit liver enzyme is not an, aberrant bisphosphatase as once believed, but is indeed homologous to, other Fru-1,6-Pases. The root-mean-square deviation of the Calpha atoms in, the rabbit liver structure from the homologous atoms in the pig kidney, structure complexed with the product, fructose 6-phosphate, is 0.7 A., Fru-1,6-Pases are homotetramers, and the rabbit liver protein crystallizes, in space group I222 with one monomer in the asymmetric unit. The structure, contains a single endogenous Mg2+ ion coordinated by Glu97, Asp118, Asp121, and Glu280 at the site designated metal site 1 in pig kidney Fru-1,6-Pase, R-form complexes. In addition, two sulfate ions, which are found at the, positions normally occupied by the 6-phosphate group of the substrate, as, well as the phosphate of the allosteric inhibitor AMP appear to provide, stability. Met177, which has hydrophobic contacts with the adenine moiety, of AMP in pig kidney T-form complexes, is replaced by glycine. Binding of, a non-hydrolyzable substrate analog, beta-methyl-fructose, 1,6-bisphosphate, at the catalytic site is also examined.
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<StructureSection load='1bk4' size='340' side='right'caption='[[1bk4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BK4 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]] 2.3&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1bk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bk4 OCA], [https://pdbe.org/1bk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1bk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bk4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F16P1_RABIT F16P1_RABIT]
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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/bk/1bk4_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=1bk4 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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1BK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG and SO4 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=1BK4 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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Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution., Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):93-102. Epub 1999, Jan 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10089399 10089399]
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[[Category: Large Structures]]
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[[Category: Fructose-bisphosphatase]]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Erman M]]
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[[Category: Erman, M.]]
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[[Category: Ghosh D]]
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[[Category: Ghosh, D.]]
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[[Category: Jornvall H]]
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[[Category: Jornvall, H.]]
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[[Category: Kaiser R]]
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[[Category: Kaiser, R.]]
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[[Category: Roszak AW]]
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[[Category: Roszak, A.W.]]
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[[Category: Weeks CM]]
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[[Category: Weeks, C.M.]]
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[[Category: MG]]
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[[Category: SO4]]
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[[Category: bisphosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:42:56 2007''
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Current revision

CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION

PDB ID 1bk4

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