2bej
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STRUCTURE OF THE BACTERIAL CHROMOSOME SEGREGATION PROTEIN SOJ
OverviewOverview
Soj and Spo0J of the Gram-negative hyperthermophile Thermus thermophilus, belong to the conserved ParAB family of bacterial proteins implicated in, plasmid and chromosome partitioning. Spo0J binds to DNA near the, replication origin and localises at the poles following initiation of, replication. Soj oscillates in the nucleoid region in an ATP- and, Spo0J-dependent fashion. Here, we show that Soj undergoes ATP-dependent, dimerisation in solution and forms nucleoprotein filaments with DNA., Crystal structures of Soj in three nucleotide states demonstrate that the, empty and ADP-bound states are monomeric, while a hydrolysis-deficient, mutant, D44A, is capable of forming a nucleotide 'sandwich' dimer. Soj, ATPase activity is stimulated by Spo0J or the N-terminal 20 amino-acid, peptide of Spo0J. Our analysis shows that dimerisation and activation, involving a peptide containing a Lys/Arg is conserved for Soj, ParA and, MinD and their modulators Spo0J, ParB and MinE, respectively. By homology, to the nitrogenase iron protein and the GTPases Ffh/FtsY, we suggest that, Soj dimerisation and regulation represent a conserved biological switch.
About this StructureAbout this Structure
2BEJ is a Single protein structure of sequence from Thermus thermophilus with MG and ADP as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch., Leonard TA, Butler PJ, Lowe J, EMBO J. 2005 Jan 26;24(2):270-82. Epub 2005 Jan 6. PMID:15635448
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