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From Proteopedia
Crystal structure of bacterial ParB dimer bound to CDP
Structural highlights
FunctionSP0J_BACSU Required for the initiation of sporulation and for normal chromosome segregation. Antagonizes sporulation inhibition by Soj. It probably interacts with a specific DNA site and other proteins involved in partitioning and cell division, and antagonizes Soj in response to cell cycle events related to chromosome partitioning.[1] Publication Abstract from PubMedParABS systems facilitate chromosome segregation and plasmid partitioning in bacteria and archaea. ParB protein binds centromeric parS DNA sequences and spreads to flanking DNA. We show that ParB is an enzyme that hydrolyzes cytidine triphosphate (CTP) to diphosphate (CDP). parS DNA stimulates cooperative CTP binding by ParB and CTP hydrolysis. A nucleotide co-crystal structure elucidates the catalytic center of the dimerization-dependent ParB CTPase. Single-molecule imaging and biochemical assays recapitulate features of ParB spreading from parS in the presence but not absence of CTP. The findings suggest that centromeres assemble by self-loading of ParB DNA sliding clamps at parS ParB CTPase is not related to known nucleotide hydrolases and might be a promising target for developing new classes of antibiotics. Self-organization of parS centromeres by the ParB CTP hydrolase.,Soh YM, Davidson IF, Zamuner S, Basquin J, Bock FP, Taschner M, Veening JW, De Los Rios P, Peters JM, Gruber S Science. 2019 Oct 24. pii: science.aay3965. doi: 10.1126/science.aay3965. PMID:31649139[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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