pyrophosphate and Lyme-Disease

pyrophosphate has been researched along with Lyme-Disease* in 1 studies

Other Studies

1 other study(ies) available for pyrophosphate and Lyme-Disease

Article	Year
The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure (London, England : 1993), 2002, Volume: 10, Issue:5 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. Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Borrelia burgdorferi; Diphosphates; Escherichia coli Proteins; Fructosephosphates; Humans; Lyme Disease; Models, Molecular; Molecular Sequence Data; Molecular Structure; Phosphofructokinases; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment	2002

Article

Year

The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.

Structure (London, England : 1993), 2002, Volume: 10, Issue:5

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.

Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Borrelia burgdorferi; Diphosphates; Escherichia coli Proteins; Fructosephosphates; Humans; Lyme Disease; Models, Molecular; Molecular Sequence Data; Molecular Structure; Phosphofructokinases; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment

2002