3IBP
The Crystal Structure of the Dimerization Domain of Escherichia coli Structural Maintenance of Chromosomes Protein MukB
Summary for 3IBP
| Entry DOI | 10.2210/pdb3ibp/pdb |
| Descriptor | Chromosome partition protein mukB, AMMONIUM ION (3 entities in total) |
| Functional Keywords | mukb, structural maintenance of chromosomes, smc, condensin, cohesin, chromosome segregation, hinge, dimerization domain, atp-binding, cell cycle, cell division, chromosome partition, dna condensation, dna-binding, nucleotide-binding |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm, nucleoid : P22523 |
| Total number of polymer chains | 1 |
| Total formula weight | 34660.67 |
| Authors | Li, Y.,Schoeffler, A.J.,Berger, J.M.,Oakley, M.G. (deposition date: 2009-07-16, release date: 2010-01-26, Last modification date: 2024-11-20) |
| Primary citation | Li, Y.,Schoeffler, A.J.,Berger, J.M.,Oakley, M.G. The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB. J.Mol.Biol., 395:11-19, 2010 Cited by PubMed Abstract: MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosomal segregation and condensation in gamma-proteobacteria. MukB and canonical SMC proteins share a characteristic five-domain structure. Globular N- and C-terminal domains interact to form an ATP-binding cassette-like ATPase or "head" domain, which is connected to a smaller dimerization or "hinge" domain by a long, antiparallel coiled coil. In addition to mediating dimerization, this hinge region has been implicated in both conformational flexibility and dynamic protein-DNA interactions. We report here the first crystallographic model of the MukB hinge domain. This model also contains approximately 20% of the coiled-coil domain, including an unusual coiled-coil deviation. These results will facilitate studies to clarify the roles of both the hinge and the coiled-coil domains in MukB function. PubMed: 19853611DOI: 10.1016/j.jmb.2009.10.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.099 Å) |
Structure validation
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