5NMO
Structure of the Bacillus subtilis Smc Joint domain
Summary for 5NMO
| Entry DOI | 10.2210/pdb5nmo/pdb |
| Descriptor | Chromosome partition protein Smc,Chromosome partition protein Smc, SULFATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total) |
| Functional Keywords | smc chromosome segregation, cell cycle |
| Biological source | Bacillus subtilis (strain 168) More |
| Cellular location | Cytoplasm : P51834 |
| Total number of polymer chains | 2 |
| Total formula weight | 40485.37 |
| Authors | Diebold-Durand, M.-L.,Basquin, J.,Gruber, S. (deposition date: 2017-04-06, release date: 2017-06-21, Last modification date: 2024-05-08) |
| Primary citation | Diebold-Durand, M.L.,Lee, H.,Ruiz Avila, L.B.,Noh, H.,Shin, H.C.,Im, H.,Bock, F.P.,Burmann, F.,Durand, A.,Basfeld, A.,Ham, S.,Basquin, J.,Oh, B.H.,Gruber, S. Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization. Mol. Cell, 67:334-347.e5, 2017 Cited by PubMed Abstract: Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase "head" and a "hinge" dimerization domain connected by a 49 nm coiled-coil "arm." The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms. PubMed: 28689660DOI: 10.1016/j.molcel.2017.06.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.899 Å) |
Structure validation
Download full validation report
