PDBsum entry 1a17

Hydrolase

PDB id: 1a17

Contents

Protein chain

159 a.a. *

Ligands

SO4 ×2

Waters ×78

* Residue conservation analysis

PDB id:

1a17

Name:

Hydrolase

Title:

Tetratricopeptide repeats of protein phosphatase 5

Structure:

Serine/threonine protein phosphatase 5. Chain: a. Fragment: protein interacting domain. Synonym: tetratricopeptide, trp. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: brain. Gene: ppp5. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_tissue: brain.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.45Å R-factor: 0.201 R-free: 0.298

Authors:

A.K.Das,P.T.W.Cohen,D.Barford

Key ref:

A.K.Das et al. (1998). The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J, 17, 1192-1199. PubMed id: 9482716 DOI: 10.1093/emboj/17.5.1192

Date:

23-Dec-97 Release date: 29-Apr-98

Protein chain

P53041  (PPP5_HUMAN) -  Serine/threonine-protein phosphatase 5 from Homo sapiens

Seq: 499 a.a.

Struc: 159 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1093/emboj/17.5.1192

EMBO J 17:1192-1199 (1998)

PubMed id: 9482716

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.

A.K.Das, P.W.Cohen, D.Barford.

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.

Selected figure(s)

Figure 1.
Figure 1 Schematic of TPR-containing proteins. TPR motifs (shown as boxes) are observed as multiple tandem repeats and also separated by sequence insertions.

Figure 2.
Figure 2 Stereo view of the electron density map of the PP5 -TPR domain calculated to 2.5 Å resolution using experimental phases with the refined coordinates superimposed. The figure was produced using O (Jones et al., 1991).

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1998, 17, 1192-1199) copyright 1998.

Figures were selected by an automated process.