8QZO
Crystal structure of heterodimeric complex of CdpB1 and CdpB2 from A. fulgidus
Summary for 8QZO
| Entry DOI | 10.2210/pdb8qzo/pdb |
| Descriptor | PRC-barrel domain-containing protein (2 entities in total) |
| Functional Keywords | divisive, cell division, archeae, bacillus subtilise, sepf, prc1, prc2, cdpb1, cdpb2, fulgidus, cell cycle |
| Biological source | Archaeoglobus fulgidus More |
| Total number of polymer chains | 4 |
| Total formula weight | 83628.41 |
| Authors | |
| Primary citation | Nussbaum, P.,Kureisaite-Ciziene, D.,Bellini, D.,van der Does, C.,Kojic, M.,Taib, N.,Yeates, A.,Tourte, M.,Gribaldo, S.,Loose, M.,Lowe, J.,Albers, S.V. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. Nat Microbiol, 9:698-711, 2024 Cited by PubMed Abstract: Cell division in all domains of life requires the orchestration of many proteins, but in Archaea most of the machinery remains poorly characterized. Here we investigate the FtsZ-based cell division mechanism in Haloferax volcanii and find proteins containing photosynthetic reaction centre (PRC) barrel domains that play an essential role in archaeal cell division. We rename these proteins cell division protein B 1 (CdpB1) and CdpB2. Depletions and deletions in their respective genes cause severe cell division defects, generating drastically enlarged cells. Fluorescence microscopy of tagged FtsZ1, FtsZ2 and SepF in CdpB1 and CdpB2 mutant strains revealed an unusually disordered divisome that is not organized into a distinct ring-like structure. Biochemical analysis shows that SepF forms a tripartite complex with CdpB1/2 and crystal structures suggest that these two proteins might form filaments, possibly aligning SepF and the FtsZ2 ring during cell division. Overall our results indicate that PRC-domain proteins play essential roles in FtsZ-based cell division in Archaea. PubMed: 38443575DOI: 10.1038/s41564-024-01600-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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