PDBsum entry 1kzh

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Transferase PDB id
Protein chains
550 a.a. *
SO4 ×8
Waters ×136
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Structure of a pyrophosphate-dependent phosphofructokinase from the lyme disease spirochete borrelia burgdorferi
Structure: Phosphofructokinase. Chain: a, b. Synonym: pyrophosphate--fructose 6-phosphate 1- phosphotransferase. Engineered: yes
Source: Borrelia burgdorferi. Lyme disease spirochete. Organism_taxid: 139. Gene: bb0020. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
2.55Å     R-factor:   0.203     R-free:   0.243
Authors: S.A.Moore,R.S.Ronimus,R.S.Roberson,H.W.Morgan
Key ref:
S.A.Moore et al. (2002). The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure, 10, 659-671. PubMed id: 12015149 DOI: 10.1016/S0969-2126(02)00760-8
06-Feb-02     Release date:   15-May-02    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P70826  (P70826_BORBG) -  Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
555 a.a.
550 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Diphosphate--fructose-6-phosphate 1-phosphotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6- bisphosphate
+ D-fructose 6-phosphate
= phosphate
+ D-fructose 1,6- bisphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     phosphorylation   4 terms 
  Biochemical function     transferase activity     6 terms  


DOI no: 10.1016/S0969-2126(02)00760-8 Structure 10:659-671 (2002)
PubMed id: 12015149  
The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
S.A.Moore, R.S.Ronimus, R.S.Roberson, H.W.Morgan.
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.
  Selected figure(s)  
Figure 2.
Figure 2. Tertiary Structure of B. burgdorferi PP[i] PFK and Comparison to E. coli PFK(A) A stereo ribbon diagram of the A subunit of B. burgdorferi PP[i] PFK showing active site residues and bound sulfate anions corresponding to the substrates drawn as stick representations with atom-type colors (oxygen red, nitrogen blue, phosphorous or sulfur yellow, and carbon gray). For convenience, only the secondary structures are labeled. See Figure 4 for an identical view of the labeled active site residues. Contributions to the active site from the neighboring B subunit are also shown.(B) A stereo ribbon diagram of the A subunit of E. coli ATP PFK drawn in an identical orientation to (A).(C) A stereo C[a] plot of the A chain of B. burgdorferi PFK in colors according to the secondary structure assignment in Figure 3 and in an identical orientation to (A). Every tenth residue is labeled.(D) A C[a] overlay of the A and B chains of B. burgdorferi PFK in green and slate blue, respectively. The helical domains and the 380-390 hairpin are labeled. (A-D) were drawn with Molscript [45] and Raster3D [46].
  The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 659-671) copyright 2002.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18231813 F.R.Lopes, M.F.Carazzolle, G.A.Pereira, C.A.Colombo, and C.M.Carareto (2008).
Transposable elements in Coffea (Gentianales: Rubiacea) transcripts and their role in the origin of protein diversity in flowering plants.
  Mol Genet Genomics, 279, 385-401.  
15668016 K.von Lackum, and B.Stevenson (2005).
Carbohydrate utilization by the Lyme borreliosis spirochete, Borrelia burgdorferi.
  FEMS Microbiol Lett, 243, 173-179.  
12595717 J.W.Keillor, C.Lherbet, R.Castonguay, D.Lapierre, J.Martinez-Oyanedel, L.A.Fothergill-Gilmore, and M.D.Walkinshaw (2003).
Expression, purification, crystallization and preliminary crystallographic analysis of Trypanosoma brucei phosphofructokinase.
  Acta Crystallogr D Biol Crystallogr, 59, 532-534.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.