Pentapeptide repeat proteins.
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.
Vetting
Matthew W
MW
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Hegde
Subray S
SS
Fajardo
J Eduardo
JE
Fiser
Andras
A
Roderick
Steven L
SL
Takiff
Howard E
HE
Blanchard
John S
JS
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001483:Base Sequence; D027081:DNA Gyrase / Q000378:metabolism; D019281:Dimerization; D004352:Drug Resistance, Microbial; D024841:Fluoroquinolones / Q000037:antagonists & inhibitors / Q000737:chemistry; D020559:Monomeric GTP-Binding Proteins; D009169:Mycobacterium tuberculosis / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D055672:Static Electricity; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D024841:Fluoroquinolones; D009842:Oligopeptides; C445685:MfpA protein, Mycobacterium smegmatis; D020559:Monomeric GTP-Binding Proteins; D027081:DNA Gyrase