4I98
Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)
Summary for 4I98
| Entry DOI | 10.2210/pdb4i98/pdb |
| Related | 4I99 |
| Descriptor | Segregation and condensation protein A, Segregation and condensation protein B (3 entities in total) |
| Functional Keywords | scpa, scpb, dna condensation, smc, cell cycle |
| Biological source | Streptococcus pneumoniae More |
| Cellular location | Cytoplasm : C1CMI6 C1CMI5 |
| Total number of polymer chains | 3 |
| Total formula weight | 59748.94 |
| Authors | Shin, H.C.,Oh, B.H. (deposition date: 2012-12-05, release date: 2013-01-30, Last modification date: 2014-12-17) |
| Primary citation | Burmann, F.,Shin, H.C.,Basquin, J.,Soh, Y.M.,Gimenez-Oya, V.,Kim, Y.G.,Oh, B.H.,Gruber, S. An asymmetric SMC-kleisin bridge in prokaryotic condensin Nat.Struct.Mol.Biol., 20:371-379, 2013 Cited by PubMed Abstract: Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes. PubMed: 23353789DOI: 10.1038/nsmb.2488 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
