1KZH

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

Summary for 1KZH

• Entry DOI: 10.2210/pdb1kzh/pdb
• Related: 1PFK
• Descriptor: phosphofructokinase, SULFATE ION (3 entities in total)
• Functional Keywords: phosphofructokinase, pyrophosphate, phosphotransferase, spirochete, borrelia burgdorferi, transferase
• Biological source: Borrelia burgdorferi
• Total number of polymer chains: 2
• Total formula weight: 125872.13

Authors

Moore, S.A.,Ronimus, R.S.,Roberson, R.S.,Morgan, H.W. (deposition date: 2002-02-06, release date: 2002-05-15, Last modification date: 2024-03-13)

Primary citation

Moore, S.A.,Ronimus, R.S.,Roberson, R.S.,Morgan, H.W.
The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
Structure, 10:659-671, 2002

PubMed 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.

PubMed: 12015149
DOI: 10.1016/S0969-2126(02)00760-8

Experimental method

X-RAY DIFFRACTION (2.55 Å)