title: Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning.
abstract: BACKGROUND
  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.
  
  
  RESULTS
  We have cloned, overexpressed and crystallized a 26 kDa protein consisting of 227 N-terminal residues of MukB from E. coli. The structure has been solved using multiple anomalous dispersion and has been refined to 2.2 A resolution. The N-terminal domain of MukB has a mixed alpha/beta fold with a central six-stranded antiparallel beta sheet. The putative nucleotide-binding loop, which is part of an unexpected helix-loop-helix motif, is exposed on the surface and no nucleotide-binding pocket could be detected.
  
  
  CONCLUSIONS
  The N-terminal domain of MukB has no similarity to the kinesin family of motor proteins or to any other nucleotide-binding protein. Together with the finding of the exposed Walker A motif this observation supports a model in which the N- and C-terminal domains come together in the dimer of MukB to form the active site. Conserved residues on one side of the molecule delineate a region of the N-terminal domain that is likely to interact with the C-terminal domain.
authors.affiliation: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
authors.forename: F
authors.initials: F
authors.lastname: van den Ent
authors.forename: A
authors.initials: A
authors.lastname: Lockhart
authors.forename: J
authors.initials: J
authors.lastname: Kendrick-Jones
authors.forename: J
authors.initials: J
authors.lastname: Löwe
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D001483:Base Sequence; D002868:Chromosomal Proteins, Non-Histone; D002876:Chromosomes, Bacterial / Q000502:physiology*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology; D029968:Escherichia coli Proteins; D015870:Gene Expression; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D002868:Chromosomal Proteins, Non-Histone; D017931:DNA Primers; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; C067035:MukB protein, E coli