Pentapeptide repeat proteins

Biochemistry. 2006 Jan 10;45(1):1-10. doi: 10.1021/bi052130w.


The pentapeptide repeat protein (PRP) family has more than 500 members in the prokaryotic and eukaryotic kingdoms. These proteins are composed of, or contain domains composed of, tandemly repeated amino acid sequences with a consensus sequence of [S,T,A,V][D,N][L,F][S,T,R][G]. The biochemical function of the vast majority of PRP family members is unknown. The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis. The structure revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral beta-helix. MfpA binds to DNA gyrase and inhibits its activity. The rod-shaped, dimeric protein exhibits remarkable similarity in size, shape, and electrostatics to DNA.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • DNA Gyrase / metabolism
  • Dimerization
  • Drug Resistance, Microbial
  • Fluoroquinolones / antagonists & inhibitors
  • Fluoroquinolones / chemistry
  • Monomeric GTP-Binding Proteins
  • Mycobacterium tuberculosis / chemistry
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Protein Conformation
  • Static Electricity
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Fluoroquinolones
  • Oligopeptides
  • MfpA protein, Mycobacterium smegmatis
  • Monomeric GTP-Binding Proteins
  • DNA Gyrase