PMID:10545328
| Citation |
van den Ent, F, Lockhart, A, Kendrick-Jones, J and Löwe, J (1999) Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning. Structure 7:1181-7 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Base Sequence; Chromosomal Proteins, Non-Histone; Chromosomes, Bacterial/physiology; Cloning, Molecular; Crystallography, X-Ray; DNA Primers/genetics; DNA, Bacterial/genetics; Dimerization; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins; Gene Expression; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Sequence Homology, Amino Acid |
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