Pentapeptide repeat proteins.

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

doi:10.1021/bi052130w

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Pentapeptide repeat proteins.

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

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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 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.

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Bacterial Proteins Base Sequence DNA Gyrase Dimerization Drug Resistance, Microbial Fluoroquinolones Monomeric GTP-Binding Proteins Mycobacterium tuberculosis Oligopeptides Protein Conformation Static Electricity Structure-Activity Relationship Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

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Matthew W Vetting, Subray S Hegde, J Eduardo Fajardo, Andras Fiser, Steven L Roderick, Howard E Takiff, John S Blanchard. 2006-01-10. Pentapeptide repeat proteins.. https://doi.org/10.1021/bi052130w

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