3ibp

Publication Abstract from PubMed

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.

The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB.,Li Y, Schoeffler AJ, Berger JM, Oakley MG J Mol Biol. 2010 Jan 8;395(1):11-9. Epub 2009 Oct 22. PMID:19853611^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.