PDBsum entry 1na0

De novo protein

PDB id: 1na0

Contents

Protein chains

119 a.a. *

Ligands

ACT

IPT ×2

Metals

_PB ×5

_CL

_NA ×2

_MG

Waters ×157

* Residue conservation analysis

PDB id:

1na0

Name:

De novo protein

Title:

Design of stable alpha-helical arrays from an idealized tpr motif

Structure:

Designed protein ctpr3. Chain: a, b. Engineered: yes

Source:

Unidentified. Organism_taxid: 32644. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.186 R-free: 0.216

Authors:

E.Main,Y.Xiong,M.Cocco,L.D'Andrea,L.Regan

Key ref:

E.R.Main et al. (2003). Design of stable alpha-helical arrays from an idealized TPR motif. Structure, 11, 497-508. PubMed id: 12737816 DOI: 10.1016/S0969-2126(03)00076-5

Date:

26-Nov-02 Release date: 03-Jun-03

Protein chains

No UniProt id for this chain

Struc: 119 a.a.

DOI no: 10.1016/S0969-2126(03)00076-5

Structure 11:497-508 (2003)

PubMed id: 12737816

Design of stable alpha-helical arrays from an idealized TPR motif.

E.R.Main, Y.Xiong, M.J.Cocco, L.D'Andrea, L.Regan.

ABSTRACT

The tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that occurs in over 300 different proteins. In the different proteins, three to sixteen or more TPR motifs occur in tandem arrays and function to mediate protein-protein interactions. The binding specificity of each TPR protein is different, although the underlying structural motif is the same. Here we describe a statistical approach to the design of an idealized TPR motif. We present the high-resolution X-ray crystal structures (to 1.55 and 1.6 A) of designed TPR proteins and describe their solution properties and stability. A detailed analysis of these structures provides an understanding of the TPR motif, how it is repeated to give helical arrays with different superhelical twists, and how a very stable framework may be constructed for future functional designs.

Selected figure(s)

Figure 3.
Figure 3. Structural Features of CTPR2/3(A) Representation of the electron density of CTPR2 in the vicinity of Tyr23(B2) and Tyr24(B2). A 2F[o] - F[c] map (blue), contoured at 1 s, is displayed over a stick model of the structure to demonstrate the quality of the data.(B-D) Representation of the overall folds of (B) CTPR2 and (C) CTPR3 and (D) a stereo view of the overlaid structures of CTPR2 (red) and CTPR3 (blue). They are represented by a tubular worm that snakes through their C^a backbones. CTPR2 (red) corresponds to 86 amino acids from Gly3 to Gly15(solvating helix), and CTPR3 (blue) corresponds to 119 amino acids from Asn2 to Gly15(solvating helix). The N and C termini are marked on each diagram.(E) An illustration showing the two IPTG molecules (space fill, purple and blue) that induce a dimer interface between two molecules of CTPR3 (rendered as a cyan and red C^a trace). The side chains of residues that interact with the IPTG are rendered as sticks, with the chloride ion caught between the two IPTG molecules rendered as green space fills. (A)-(E) were produced with SPOCK [53].

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 497-508) copyright 2003.

Figure was selected by an automated process.