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3IBP

The Crystal Structure of the Dimerization Domain of Escherichia coli Structural Maintenance of Chromosomes Protein MukB

Summary for 3IBP
Entry DOI10.2210/pdb3ibp/pdb
DescriptorChromosome partition protein mukB, AMMONIUM ION (3 entities in total)
Functional Keywordsmukb, 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 sourceEscherichia coli
Cellular locationCytoplasm, nucleoid : P22523
Total number of polymer chains1
Total formula weight34660.67
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 citationLi, 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: 19853611
DOI: 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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数据于2025-11-19公开中

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