1kzh

From Proteopedia

(Difference between revisions)

Revision as of 11:03, 12 October 2017

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

Structural highlights

1kzh is a 2 chain structure with sequence from Atcc 35210. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1pfk
Gene:	BB0020 (ATCC 35210)
Activity:	Diphosphate--fructose-6-phosphate 1-phosphotransferase, with EC number 2.7.1.90
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deng Z, Roberts D, Wang X, Kemp RG. Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi. Arch Biochem Biophys. 1999 Nov 15;371(2):326-31. PMID:10545221 doi:http://dx.doi.org/10.1006/abbi.1999.1446
↑ Moore SA, Ronimus RS, Roberson RS, Morgan HW. The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure. 2002 May;10(5):659-71. PMID:12015149

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kzh"

@@ Line 1: / Line 1: @@
 ==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi==
 <StructureSection load='1kzh' size='340' side='right' caption='[[1kzh]], [[Resolution|resolution]] 2.55&Aring;' 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='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>
 == Function ==
@@ Line 31: / Line 32: @@
 </div>
 <div class="pdbe-citations 1kzh" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Phosphofructokinase (PFK)|Phosphofructokinase (PFK)]]
 == References ==
 <references/>

1kzh

From Proteopedia

Revision as of 11:03, 12 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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