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1kzh
From Proteopedia
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Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
Overview
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 Structure
1KZH is a Single protein structure of sequence from Borrelia burgdorferi with SO4 as ligand. Active as Diphosphate--fructose-6-phosphate 1-phosphotransferase, with EC number 2.7.1.90 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 25 02:13:44 2007
