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4DZZ

Structure of ParF-ADP, crystal form 1

Summary for 4DZZ
Entry DOI10.2210/pdb4dzz/pdb
Related4E03 4E07 4E09
DescriptorPlasmid partitioning protein ParF, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsdeviant walker box, dna segregation, unknown function
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight45025.62
Authors
Schumacher, M.A.,Ye, Q.,Barge, M.R.,Barilla, D.,Hayes, F. (deposition date: 2012-03-01, release date: 2012-06-13, Last modification date: 2024-02-28)
Primary citationSchumacher, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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