PDBsum entry 6sdk

DNA binding protein

PDB id: 6sdk

Contents

Protein chains

199 a.a.

Ligands

CDP ×4

Metals

_CA ×8

Waters ×495

PDB id:

6sdk

Name:

DNA binding protein

Title:

Crystal structure of bacterial parb dimer bound to cdp

Structure:

Stage 0 sporulation protein j. Chain: a, b, c, d. Engineered: yes

Source:

Bacillus subtilis (strain 168). Organism_taxid: 224308. Strain: 168. Gene: spo0j, bsu40960. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.81Å R-factor: 0.185 R-free: 0.213

Authors:

Y.M.Soh,J.Basquin,S.Gruber

Key ref:

Y.M.Soh et al. (2019). Self-organization of parS centromeres by the ParB CTP hydrolase. Science, 366, 1129-1133. PubMed id: 31649139 DOI: 10.1126/science.aay3965

Date:

28-Jul-19 Release date: 23-Oct-19

Protein chains

P26497  (SP0J_BACSU) -  Stage 0 sporulation protein J from Bacillus subtilis (strain 168)

Seq: 282 a.a.

Struc: 199 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1126/science.aay3965

Science 366:1129-1133 (2019)

PubMed id: 31649139

Self-organization of parS centromeres by the ParB CTP hydrolase.

Y.M.Soh, I.F.Davidson, S.Zamuner, J.Basquin, F.P.Bock, M.Taschner, J.W.Veening, P.De Los Rios, J.M.Peters, S.Gruber.

ABSTRACT

ParABS 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 cytidine diphosphate (CDP). parS 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 parS in the presence but not absence of CTP. These 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.