1kzh: Difference between revisions

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-[[Image:1kzh.jpg|left|200px]]
- {{Structure
+==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi==
-|PDB= 1kzh |SIZE=350|CAPTION= <scene name='initialview01'>1kzh</scene>, resolution 2.55&Aring;
+<StructureSection load='1kzh' size='340' side='right'caption='[[1kzh]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<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>
-|ACTIVITY= [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]
+</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>
-|GENE= BB0020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi])
+<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>
-}}
+<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>
+</table>
+== Function ==
+[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>
+== 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/kz/1kzh_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=1kzh ConSurf].
+<div style="clear:both"></div>
-'''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''
+==See Also==
+*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Borreliella burgdorferi]]
-KZH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA].
+[[Category: Large Structures]]
+[[Category: Moore SA]]
-==Reference==
+[[Category: Morgan HW]]
-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://www.ncbi.nlm.nih.gov/pubmed/12015149 12015149]
+[[Category: Roberson RS]]
-[[Category: Borrelia burgdorferi]]
+[[Category: Ronimus RS]]
-[[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]]
-[[Category: Single protein]]
-[[Category: Moore, S A.]]
-[[Category: Morgan, H W.]]
-[[Category: Roberson, R S.]]
-[[Category: Ronimus, R S.]]
-[[Category: SO4]]
-[[Category: borrelia burgdorferi]]
-[[Category: phosphofructokinase]]
-[[Category: phosphotransferase]]
-[[Category: pyrophosphate]]
-[[Category: spirochete]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:16 2008''