1kzh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi== | ==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi== | ||
<StructureSection load='1kzh' size='340' side='right' caption='[[1kzh]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='1kzh' size='340' side='right' caption='[[1kzh]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
| Line 8: | Line 9: | ||
<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='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='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='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://oca.weizmann.ac.il/oca-docs/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]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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> | </table> | ||
== Function == | == Function == | ||
| Line 31: | Line 32: | ||
</div> | </div> | ||
<div class="pdbe-citations 1kzh" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1kzh" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:03, 12 October 2017
Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferiStructure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
Structural highlights
Function[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][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||||||