Vetting Matthew W, Hegde Subray S, Fajardo J Eduardo, Fiser Andras, Roderick Steven L, Takiff Howard E, Blanchard John S
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
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.
五肽重复蛋白(PRP)家族在原核生物和真核生物界中有500多个成员。这些蛋白质由串联重复的氨基酸序列组成,或包含由串联重复氨基酸序列组成的结构域,共有序列为[S,T,A,V][D,N][L,F][S,T,R][G]。绝大多数PRP家族成员的生化功能尚不清楚。PRP家族第一个成员的三维结构是针对结核分枝杆菌的氟喹诺酮抗性蛋白(MfpA)确定的。该结构表明,五肽重复序列编码一种新型右手四边形β-螺旋的折叠。MfpA与DNA回旋酶结合并抑制其活性。这种杆状二聚体蛋白在大小、形状和静电方面与DNA表现出显著相似性。