4E09

Structure of ParF-AMPPCP, I422 form

Summary for 4E09

• Entry DOI: 10.2210/pdb4e09/pdb
• Related: 4DZZ 4E03 4E07
• Descriptor: Plasmid partitioning protein ParF, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, SULFATE ION (3 entities in total)
• Functional Keywords: deviant walker box, dna segregation, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 22662.57

Authors

Schumacher, M.A.,Ye, Q.,Barge, M.R.,Barilla, D.,Hayes, F. (deposition date: 2012-03-02, release date: 2012-06-13, Last modification date: 2024-02-28)

Primary citation

Schumacher, M.A.,Ye, Q.,Barge, M.T.,Zampini, M.,Barilla, D.,Hayes, F.
Structural Mechanism of ATP-induced Polymerization of the Partition Factor ParF: IMPLICATIONS FOR DNA SEGREGATION.
J.Biol.Chem., 287:26146-26154, 2012

PubMed Abstract: Segregation of the bacterial multidrug resistance plasmid TP228 requires the centromere-binding protein ParG, the parH centromere, and the Walker box ATPase ParF. The cycling of ParF between ADP- and ATP-bound states drives TP228 partition; ATP binding stimulates ParF polymerization, which is essential for segregation, whereas ADP binding antagonizes polymerization and inhibits DNA partition. The molecular mechanism involved in this adenine nucleotide switch is unclear. Moreover, it is unknown how any Walker box protein polymerizes in an ATP-dependent manner. Here, we describe multiple ParF structures in ADP- and phosphomethylphosphonic acid adenylate ester (AMPPCP)-bound states. ParF-ADP is monomeric but dimerizes when complexed with AMPPCP. Strikingly, in ParF-AMPPCP structures, the dimers interact to create dimer-of-dimer "units" that generate a specific linear filament. Mutation of interface residues prevents both polymerization and DNA segregation in vivo. Thus, these data provide insight into a unique mechanism by which a Walker box protein forms polymers that involves the generation of ATP-induced dimer-of-dimer building blocks.

PubMed: 22674577
DOI: 10.1074/jbc.M112.373696

Experimental method

X-RAY DIFFRACTION (2.99 Å)