1kzh: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1kzh' size='340' side='right'caption='[[1kzh]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1KZH FirstGlance]. <br>
+<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>
-</td></tr><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>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pfk|1pfk]]</div></td></tr>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BB0020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 ATCC 35210])</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzh OCA], [http://pdbe.org/1kzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kzh RCSB], [http://www.ebi.ac.uk/pdbsum/1kzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A0H3C4C8_BORBZ A0A0H3C4C8_BORBZ]] 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]
+[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]]
@@ Line 22: / Line 20: @@
 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:12015149<ref>PMID:12015149</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1kzh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 38: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 35210]]
+[[Category: Borreliella burgdorferi]]
-[[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]]
 [[Category: Large Structures]]
-[[Category: Moore, S A]]
+[[Category: Moore SA]]
-[[Category: Morgan, H W]]
+[[Category: Morgan HW]]
-[[Category: Roberson, R S]]
+[[Category: Roberson RS]]
-[[Category: Ronimus, R S]]
+[[Category: Ronimus RS]]
-[[Category: Borrelia burgdorferi]]
-[[Category: Phosphofructokinase]]
-[[Category: Phosphotransferase]]
-[[Category: Pyrophosphate]]
-[[Category: Spirochete]]
-[[Category: Transferase]]