Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb

Mol Microbiol. 2007 Mar;63(5):1319-30. doi: 10.1111/j.1365-2958.2007.05586.x. Epub 2007 Jan 22.


The genome of the Lyme disease-causing spirochete Borrelia burgdorferi encodes only a single polypeptide from the integration host factor (IHF)/HU or 'DNABII' family of nucleoid-associated proteins - Hbb. DNABII proteins induce large bends in DNA and serve as architectural factors in a variety of prokaryotic cellular processes. We have solved the crystal structure of an Hbb-DNA complex in which the DNA is bent by over 180 degrees . We find that like IHF, Hbb relies exclusively on indirect readout to recognize its cognate site. Additional binding studies show that the sequence preferences of Hbb are related to, yet distinct from those of IHF. Defining these binding characteristics may help to uncover additional roles for Hbb in Borrelia DNA metabolism as well as further our understanding of the mechanism of indirect readout.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Borrelia burgdorferi / chemistry*
  • Borrelia burgdorferi / genetics
  • Crystallography, X-Ray
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Genome, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Substrate Specificity


  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Hbb protein, Borrelia burgdorferi

Associated data

  • PDB/2NP2