1zxx

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(New page: 200px<br /><applet load="1zxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zxx, resolution 1.85&Aring;" /> '''The crystal structur...)
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[[Image:1zxx.gif|left|200px]]<br /><applet load="1zxx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zxx, resolution 1.85&Aring;" />
 
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'''The crystal structure of phosphofructokinase from Lactobacillus delbrueckii'''<br />
 
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==Overview==
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==The crystal structure of phosphofructokinase from Lactobacillus delbrueckii==
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Phosphofructokinase from Lactobacillus delbrueckii subspecies bulgaricus, (LbPFK) has been reported to be a nonallosteric analogue of, phosphofructokinase from Escherichia coli at pH 8.2 [Le Bras et al. (1991), Eur. J. Biochem. 198, 683-687]. A reexamination of the kinetics of this, enzyme shows LbPFK to have limited binding affinity toward the allosteric, ligands, MgADP and PEP, with dissociation constants of approximately 20 mM, for both. Their allosteric effects are observed only at high, concentrations of these ligands, with both exhibiting inhibitory effects, on substrate binding. No pH dependence was observed for the binding and, the influence of MgADP and PEP on the enzyme. To attempt to explain these, results, the crystal structure of LbPFK was solved using molecular, replacement to 1.86 A resolution. A comparative study of the LbPFK, structure with that of phosphofructokinases from E. coli (EcPFK) and, Bacillus stearothermophilus (BsPFK) reveals a structure with conserved, fold and substrate binding site. The effector binding site, however, shows, many differences that could explain the observed decreases in binding, affinity for MgADP and PEP in LbPFK as compared to the other two enzymes.
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<StructureSection load='1zxx' size='340' side='right'caption='[[1zxx]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus Lactobacillus delbrueckii subsp. bulgaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXX 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]] 1.85&#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=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=1zxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxx OCA], [https://pdbe.org/1zxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxx RCSB], [https://www.ebi.ac.uk/pdbsum/1zxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PFKA_LACDE PFKA_LACDE] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]<ref>PMID:1828763</ref>
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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/zx/1zxx_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=1zxx 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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1ZXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus Lactobacillus delbrueckii subsp. bulgaricus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZXX OCA].
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*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus., Paricharttanakul NM, Ye S, Menefee AL, Javid-Majd F, Sacchettini JC, Reinhart GD, Biochemistry. 2005 Nov 22;44(46):15280-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16285731 16285731]
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__TOC__
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[[Category: 6-phosphofructokinase]]
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</StructureSection>
[[Category: Lactobacillus delbrueckii subsp. bulgaricus]]
[[Category: Lactobacillus delbrueckii subsp. bulgaricus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Javid-Majd, F.]]
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[[Category: Javid-Majd F]]
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[[Category: Menefee, A.L.]]
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[[Category: Menefee AL]]
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[[Category: Paricharttanakul, N.M.]]
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[[Category: Paricharttanakul NM]]
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[[Category: Reinhart, G.D.]]
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[[Category: Reinhart GD]]
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[[Category: Sacchettini, J.C.]]
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[[Category: Sacchettini JC]]
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[[Category: Ye, S.]]
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[[Category: Ye S]]
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[[Category: SO4]]
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[[Category: allosteric regulation]]
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[[Category: lactobacillus bulgaricus]]
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[[Category: phosphofructokinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:43:33 2007''
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Current revision

The crystal structure of phosphofructokinase from Lactobacillus delbrueckii

PDB ID 1zxx

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