1A17
TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5
Summary for 1A17
| Entry DOI | 10.2210/pdb1a17/pdb |
| Descriptor | SERINE/THREONINE PROTEIN PHOSPHATASE 5, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, phosphatase, protein-protein interactions, tpr, super-helix |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus : P53041 |
| Total number of polymer chains | 1 |
| Total formula weight | 19252.67 |
| Authors | Das, A.K.,Cohen, P.T.W.,Barford, D. (deposition date: 1997-12-23, release date: 1998-04-29, Last modification date: 2024-02-07) |
| Primary citation | Das, A.K.,Cohen, P.W.,Barford, D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J., 17:1192-1199, 1998 Cited by PubMed Abstract: The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a wide variety of proteins, present in tandem arrays of 3-16 motifs, which form scaffolds to mediate protein-protein interactions and often the assembly of multiprotein complexes. TPR-containing proteins include the anaphase promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67 phox, hsp90-binding immunophilins, transcription factors, the PKR protein kinase inhibitor, and peroxisomal and mitochondrial import proteins. Here, we report the crystal structure of the TPR domain of a protein phosphatase, PP5. Each of the three TPR motifs of this domain consist of a pair of antiparallel alpha-helices of equivalent length. Adjacent TPR motifs are packed together in a parallel arrangement such that a tandem TPR motif structure is composed of a regular series of antiparallel alpha-helices. The uniform angular and spatial arrangement of neighbouring alpha-helices defines a helical structure and creates an amphipathic groove. Multiple-TPR motif proteins would fold into a right-handed super-helical structure with a continuous helical groove suitable for the recognition of target proteins, hence defining a novel mechanism for protein recognition. The spatial arrangement of alpha-helices in the PP5-TPR domain is similar to those within 14-3-3 proteins. PubMed: 9482716DOI: 10.1093/emboj/17.5.1192 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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