Pentapeptide repeat

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Pentapeptide repeat
Structure of the pentapeptide repeat protein HetL.[1]
Identifiers
SymbolPentapeptide
PfamPF00805
InterProIPR001646
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB2bm4​, 2bm5​, 2bm6​, 2bm7​, 2w7z​, 3du1​, PDB: 2O6W​, PDB: 2J8K​, PDB: 2J8I

Pentapeptide repeats are a family of sequence motifs found in multiple tandem copies in protein molecules.[2][3] Pentapeptide repeat proteins are found in all species, but they are found in many copies in cyanobacterial genomes. The repeats were first identified by Black and colleagues in the hglK protein.[4] The later Bateman et al. showed that a large family of related pentapeptide repeat proteins existed.[3] The function of these repeats is uncertain in most proteins. However, in the MfpA protein a DNA gyrase inhibitor it has been suggested that the pentapeptide repeat structure mimics the structure of DNA.[5] The repeats form a regular right handed four sided beta helix structure known as the Rfr-fold.

Sequence features

Multiple sequence alignment of pentapeptide repeat proteins.
Dot plot of the HglK protein against itself showing repeats as diagonal lines.

The pentapeptide repeat is a feature seen in

protein sequence. It can be approximately described using the 1-letter amino acid code as A(D/N)LXX, where X can be any amino acid . This repeating sequence can be seen in multiple sequence alignments and dot plots
of proteins such as HglK. The central position in the pentapeptide repeat is usually a leucine and has been designated as position i. The two previous positions are known as i-1 and i-2. Position i-2 is usually an alanine. The two subsequent positions are denoted i+1 and i+2. The side chains of positions i-2 and i point into the hydrophobic interior of the protein while the side chains of positions i-1, i+1 and i+2 are exposed on the surface of the proteins.

Structure

Pentapeptide repeats were initially predicted from sequence to possess a right handed beta helix with three sides.[3] The first crystal structure of a pentapeptide repeat protein was the MfpA protein solved by Hegde and colleagues. It showed that pentapeptide repeat proteins (PRPs) possessed a four sided beta helix structure.[5] Four repeats make up one turn of a solenoid like structure. The structures of eight different proteins have been solved to date.

Protein PDB code Length Number of repeats Reference
Mycobacterium tuberculosis MfpA PDB: 2bm4 183 30 [5]
Cyanobacterium nostoc HetL PDB: 3du1 237 40 [1]
Enterococcus faecalis EfsQnr PDB: 2w7z 211 [6]
Nostoc punctiforme Np275 PDB: 2J8I 98 17 [7]
Nostoc punctiforme Np276 PDB: 2J8K 75 12 [7]
Cyanothece sp. Rfr32 PDB: 2F3LPDB: 2G0Y 167 21 [8]
Cyanothece sp. Rfr23 PDB: 2O6W 174 23 [9]
Arabidopsis thaliana At2g44920 PDB: 3N90 224 25 [10]

References