1T98
Crystal Structure of MukF(1-287)
Summary for 1T98
| Entry DOI | 10.2210/pdb1t98/pdb |
| Descriptor | Chromosome partition protein mukF (1 entity in total) |
| Functional Keywords | winged helix, helix-turn helix, domain swapped, condensin, cell cycle |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm, nucleoid: P60293 |
| Total number of polymer chains | 2 |
| Total formula weight | 66072.48 |
| Authors | Fennell-Fezzie, R.,Berger, J.M. (deposition date: 2004-05-14, release date: 2005-05-24, Last modification date: 2024-11-20) |
| Primary citation | Fennell-Fezzie, R.,Gradia, S.D.,Akey, D.,Berger, J.M. The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins. Embo J., 24:1921-1930, 2005 Cited by PubMed 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. PubMed: 15902272DOI: 10.1038/sj.emboj.7600680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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