6SDK
Crystal structure of bacterial ParB dimer bound to CDP
Summary for 6SDK
| Entry DOI | 10.2210/pdb6sdk/pdb |
| Descriptor | Stage 0 sporulation protein J, CYTIDINE-5'-DIPHOSPHATE, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | parb, chromosome segregation, chromosome organization, dna binding protein |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 4 |
| Total formula weight | 93144.88 |
| Authors | Soh, Y.M.,Basquin, J.,Gruber, S. (deposition date: 2019-07-28, release date: 2019-10-23, Last modification date: 2024-11-06) |
| Primary citation | Soh, Y.M.,Davidson, I.F.,Zamuner, S.,Basquin, J.,Bock, F.P.,Taschner, M.,Veening, J.W.,De Los Rios, P.,Peters, J.M.,Gruber, S. Self-organization ofparScentromeres by the ParB CTP hydrolase. Science, 366:1129-1133, 2019 Cited by PubMed Abstract: ParABS systems facilitate chromosome segregation and plasmid partitioning in bacteria and archaea. ParB protein binds centromeric DNA sequences and spreads to flanking DNA. We show that ParB is an enzyme that hydrolyzes cytidine triphosphate (CTP) to cytidine diphosphate (CDP). DNA stimulates cooperative CTP binding by ParB and CTP hydrolysis. A nucleotide cocrystal structure elucidates the catalytic center of the dimerization-dependent ParB CTPase. Single-molecule imaging and biochemical assays recapitulate features of ParB spreading from in the presence but not absence of CTP. These findings suggest that centromeres assemble by self-loading of ParB DNA sliding clamps at ParB CTPase is not related to known nucleotide hydrolases and might be a promising target for developing new classes of antibiotics. PubMed: 31649139DOI: 10.1126/science.aay3965 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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