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1kzh

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(New page: 200px<br /><applet load="1kzh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kzh, resolution 2.55&Aring;" /> '''Structure of a pyrop...)
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[[Image:1kzh.jpg|left|200px]]<br /><applet load="1kzh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kzh, resolution 2.55&Aring;" />
 
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'''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''<br />
 
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==Overview==
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==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi==
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The structure of the 60 kDa pyrophosphate (PP(i))-dependent, phosphofructokinase (PFK) from Borrelia burgdorferi has been solved and, refined (R(free) = 0.243) at 2.55 A resolution. The domain structure of, eubacterial ATP-dependent PFKs is conserved in B. burgdorferi PFK, and, there are three large insertions relative to E. coli PFK, including a, helical domain containing a hairpin structure that interacts with the, active site. Asp177, conserved in all PP(i) PFKs, negates the binding of, the alpha-phosphate group of ATP and likely contacts the essential Mg(2+), cation via a water molecule. Asn181 blocks the binding of the adenine, moiety of ATP. Lys203 hydrogen bonds to a sulfate anion that likely mimics, PP(i) substrate binding.
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<StructureSection load='1kzh' size='340' side='right'caption='[[1kzh]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KZH 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]] 2.55&#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=1kzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzh OCA], [https://pdbe.org/1kzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kzh RCSB], [https://www.ebi.ac.uk/pdbsum/1kzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PFP_BORBU PFP_BORBU] Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01980]<ref>PMID:10545221</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/kz/1kzh_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=1kzh 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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1KZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Diphosphate--fructose-6-phosphate_1-phosphotransferase Diphosphate--fructose-6-phosphate 1-phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.90 2.7.1.90] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KZH 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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The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi., Moore SA, Ronimus RS, Roberson RS, Morgan HW, Structure. 2002 May;10(5):659-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12015149 12015149]
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__TOC__
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[[Category: Borrelia burgdorferi]]
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</StructureSection>
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[[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]]
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[[Category: Borreliella burgdorferi]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Moore, S.A.]]
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[[Category: Moore SA]]
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[[Category: Morgan, H.W.]]
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[[Category: Morgan HW]]
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[[Category: Roberson, R.S.]]
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[[Category: Roberson RS]]
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[[Category: Ronimus, R.S.]]
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[[Category: Ronimus RS]]
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[[Category: SO4]]
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[[Category: borrelia burgdorferi]]
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[[Category: phosphofructokinase]]
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[[Category: phosphotransferase]]
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[[Category: pyrophosphate]]
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[[Category: spirochete]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:13:44 2007''
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Current revision

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

PDB ID 1kzh

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