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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Amino Acid Sequence
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / physiology
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Chromatography, Affinity
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Chromosomal Proteins, Non-Histone / chemistry
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Chromosomal Proteins, Non-Histone / metabolism
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Crystallography, X-Ray
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DNA-Binding Proteins / chemistry*
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Dimerization
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Escherichia coli / chemistry*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / metabolism
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Escherichia coli Proteins / physiology
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Models, Molecular
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Molecular Sequence Data
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Multigene Family
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Multiprotein Complexes
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Protein Binding
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Protein Conformation
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Protein Interaction Mapping
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Protein Structure, Tertiary
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Repressor Proteins / chemistry
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Repressor Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
Substances
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Cell Cycle Proteins
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Chromosomal Proteins, Non-Histone
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DNA-Binding Proteins
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Escherichia coli Proteins
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MukB protein, E coli
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Multiprotein Complexes
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Repressor Proteins
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condensin complexes
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mukE protein, E coli
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mukF protein, E coli
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Adenosine Triphosphatases