Pentapeptide repeat proteins

Matthew W. Vetting, Subray S. Hegde, J. Eduardo Fajardo, Andras Fiser, Steven L. Roderick, Howard E. Takiff, John S. Blanchard

Research output: Contribution to journalReview articlepeer-review

115 Scopus citations

Abstract

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 β-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.

Original languageEnglish (US)
Pages (from-to)1-10
Number of pages10
JournalBiochemistry
Volume45
Issue number1
DOIs
StatePublished - Jan 10 2006

ASJC Scopus subject areas

  • Biochemistry

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