| Literature DB >> 12015149 |
Stanley A Moore1, Ron S Ronimus, Russel S Roberson, Hugh W Morgan.
Abstract
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.Entities:
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Year: 2002 PMID： 12015149 DOI： 10.1016/s0969-2126(02)00760-8
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006