7v8p | pdb_00007v8p
Crystal Structure of the MukE dimer
Structural highlights
FunctionMUKE_SHIFL Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF.[HAMAP-Rule:MF_01802] Publication Abstract from PubMedThe SMC (structural maintenance of chromosomes) proteins are known to be involved in chromosome pairing or aggregation and play an important role in cell cycle and division. Different from SMC-ScpAB complex maintaining chromosome structure in most bacteria, the MukB-MukE-MukF complex is responsible for chromosome condensation in E. coli and some gamma-proteobacter. Though different models were proposed to illustrate the mechanism of how the MukBEF complex worked, the assembly of the MukBEF complex is a key. The MukE dimer interacted with the middle region of one MukF molecule, and was clamped by the N- and C-terminal domain of the latter, and then was involved in the interaction with the head domain of MukB. To reveal the structural basis of MukE involved in the dynamic equilibrium of potential different MukBEF assemblies, we determined the MukE structure at 2.44 A resolution. We found that the binding cavity for the alpha10, beta4 and beta5 of MukF (residues 296-327) in the MukE dimer has been occupied by the alpha9 and beta7 strand of MukE. We proposed that the highly dynamic C-terminal region (173-225) was important for the MukE-F assembly and then involved in the MukBEF complex formation. Crystal structure of the chromosome partition protein MukE homodimer.,Qian JW, Wang XY, Deng K, Li DF, Guo L Biochem Biophys Res Commun. 2021 Dec 14;589:229-233. doi:, 10.1016/j.bbrc.2021.12.032. PMID:34929446[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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