SSF48452

TPR-like

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR011990

The domain represented in this superfamily consists of a multi-helical fold comprised of two curved layers of α-helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis
[1]
. These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. The TPR is likely to be an ancient repeat, since it is found in eukaryotes, bacteria and archaea, whereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions, and has the ability to acquire multiple functional roles
[2]
.

The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins
[3, 4, 5]
. It mediates protein-protein interactions and the assembly of multiprotein complexes
[6]
. The TPR motif consists of 3-16 tandem-repeats of 34 amino acids residues, although individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms, ranging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes, such as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.

The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helix-turn-helix arrangement, with adjacent TPR motifs packing in a parallel fashion, resulting in a spiral of repeating anti-parallel α-helices
[6]
. The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24 degrees within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A' of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A, and the other surface presents residues from both helices A and B.

References
Imported from IPR011990

1.Topological characteristics of helical repeat proteins. Groves MR, Barford D. Curr. Opin. Struct. Biol. 9, 383-9, (1999). View articlePMID: 10361086

2.Protein repeats: structures, functions, and evolution. Andrade MA, Perez-Iratxeta C, Ponting CP. J. Struct. Biol. 134, 117-31, (2001). View articlePMID: 11551174

3.Tetratrico peptide repeat interactions: to TPR or not to TPR? Lamb JR, Tugendreich S, Hieter P. Trends Biochem. Sci. 20, 257-9, (1995). View articlePMID: 7667876

4.The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. Das AK, Cohen PW, Barford D. EMBO J. 17, 1192-9, (1998). View articlePMID: 9482716

5.The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Goebl M, Yanagida M. Trends Biochem. Sci. 16, 173-7, (1991). View articlePMID: 1882418

6.TPR proteins: the versatile helix. D'Andrea LD, Regan L. Trends Biochem. Sci. 28, 655-62, (2003). View articlePMID: 14659697

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