The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
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.
Moore
Stanley A
SA
Institute of Molecular Biosciences and Allan Wilson Centre for Molecular Ecology and Evolution, Massey University, Palmerston North, New Zealand. s.morre@massey.ac.nz
Ronimus
Ron S
RS
Roberson
Russel S
RS
Morgan
Hugh W
HW
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D025065:Borrelia burgdorferi / Q000201:enzymology* / Q000235:genetics; D011756:Diphosphates / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D005636:Fructosephosphates / Q000378:metabolism; D006801:Humans; D008193:Lyme Disease / Q000382:microbiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D025221:Phosphofructokinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D001426:Bacterial Proteins; D011756:Diphosphates; D029968:Escherichia coli Proteins; D005636:Fructosephosphates; C027618:fructose-6-phosphate; D025221:Phosphofructokinases