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  • Title: The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB.
    Author: Li Y, Schoeffler AJ, Berger JM, Oakley MG.
    Journal: J Mol Biol; 2010 Jan 08; 395(1):11-9. PubMed ID: 19853611.
    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.
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