1QHL
CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF MUKB AT 2.2A RESOLUTION
Summary for 1QHL
| Entry DOI | 10.2210/pdb1qhl/pdb |
| Descriptor | PROTEIN (CELL DIVISION PROTEIN MUKB) (2 entities in total) |
| Functional Keywords | mukb, smc, chromosome partitioning, cell division protein |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm, nucleoid: P22523 |
| Total number of polymer chains | 1 |
| Total formula weight | 25246.98 |
| Authors | van den Ent, F.,Lowe, J. (deposition date: 1999-05-17, release date: 1999-11-10, Last modification date: 2023-12-27) |
| Primary citation | van den Ent, F.,Lockhart, A.,Kendrick-Jones, J.,Lowe, J. Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning. Structure Fold.Des., 7:1181-1187, 1999 Cited by PubMed Abstract: The 170 kDa protein MukB has been implicated in ATP-dependent chromosome partitioning during cell division in Escherichia coli. MukB shares its dimeric structure and domain architecture with the ubiquitous family of SMC (structural maintenance of chromosomes) proteins that facilitate similar functions. The N-terminal domain of MukB carries a putative Walker A nucleotide-binding region and the C-terminal domain has been shown to bind to DNA. Mutant phenotypes and a domain arrangement similar to motor proteins that move on microtubules led to the suggestion that MukB might be a motor protein acting on DNA. PubMed: 10545328DOI: 10.1016/S0969-2126(00)80052-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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