1kzh
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| , resolution 2.55Å | |||||||
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| Ligands: | , | ||||||
| Gene: | BB0020 (Borrelia burgdorferi) | ||||||
| Activity: | Diphosphate--fructose-6-phosphate 1-phosphotransferase, with EC number 2.7.1.90 | ||||||
| Related: | 1PFK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
OverviewOverview
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.
About this StructureAbout this Structure
1KZH is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
ReferenceReference
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
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