PMID:15902272
| Citation |
Fennell-Fezzie, R, Gradia, SD, Akey, D and Berger, JM (2005) The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins. EMBO J. 24:1921-30 |
|---|---|
| Abstract |
The Escherichia coli MukB, MukE, and MukF proteins form a bacterial condensin (MukBEF) that contributes to chromosome management by compacting DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily; however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds into a winged-helix domain and an extended coiled-coil domain that self-associate to form a stable, doubly domain-swapped dimer. Protein dissection and affinity purification data demonstrate that the region of MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit for E. coli condensin and suggest a means by which it may organize the MukBEF assembly. |
| Links |
PubMed PMC1142612 Online version:10.1038/sj.emboj.7600680 |
| Keywords |
Adenosine Triphosphatases/chemistry; Amino Acid Sequence; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/physiology; Chromatography, Affinity; Chromosomal Proteins, Non-Histone/chemistry; Chromosomal Proteins, Non-Histone/metabolism; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Dimerization; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/physiology; Models, Molecular; Molecular Sequence Data; Multigene Family; Multiprotein Complexes; Protein Binding; Protein Conformation; Protein Interaction Mapping; Protein Structure, Tertiary; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship |
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