7NG0
Crystal structure of N- and C-terminally truncated Geobacillus thermoleovorans nucleoid occlusion protein Noc
Summary for 7NG0
| Entry DOI | 10.2210/pdb7ng0/pdb |
| Descriptor | Nucleoid occlusion protein, SULFATE ION (2 entities in total) |
| Functional Keywords | ctp switch, chromosome segregation, protein-dna recognition, peripheral membrane protein, dna binding protein |
| Biological source | Geobacillus thermoleovorans CCB_US3_UF5 |
| Total number of polymer chains | 1 |
| Total formula weight | 26489.82 |
| Authors | Jalal, A.S.B.,Tran, N.T.,Wu, L.J.,Ramakrishnan, K.,Rejzek, M.,Stevenson, C.E.M.,Lawson, D.M.,Errington, J.,Le, T.B.K. (deposition date: 2021-02-08, release date: 2021-02-17, Last modification date: 2024-01-31) |
| Primary citation | Jalal, A.S.B.,Tran, N.T.,Wu, L.J.,Ramakrishnan, K.,Rejzek, M.,Gobbato, G.,Stevenson, C.E.M.,Lawson, D.M.,Errington, J.,Le, T.B.K. CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc. Mol.Cell, 81:3623-3636.e6, 2021 Cited by PubMed Abstract: ATP- and GTP-dependent molecular switches are extensively used to control functions of proteins in a wide range of biological processes. However, CTP switches are rarely reported. Here, we report that a nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly regulated by a CTP switch. In Bacillus subtilis, Noc nucleates on 16 bp NBS sites before associating with neighboring non-specific DNA to form large membrane-associated nucleoprotein complexes to physically occlude assembly of the cell division machinery. By in vitro reconstitution, we show that (1) CTP is required for Noc to form the NBS-dependent nucleoprotein complex, and (2) CTP binding, but not hydrolysis, switches Noc to a membrane-active state. Overall, we suggest that CTP couples membrane-binding activity of Noc to nucleoprotein complex formation to ensure productive recruitment of DNA to the bacterial cell membrane for nucleoid occlusion activity. PubMed: 34270916DOI: 10.1016/j.molcel.2021.06.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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