PDBsum entry 3kd7

De novo protein

PDB id: 3kd7

Contents

Protein chains

102 a.a. *

Ligands

ACE-MET-GLU-GLU-VAL-ASP ×5

Waters ×17

* Residue conservation analysis

PDB id:

3kd7

Name:

De novo protein

Title:

Designed tpr module (ctpr390) in complex with its peptide-ligand (hsp90 peptide)

Structure:

Ctpr390. Chain: a, b, c, d, e. Engineered: yes. Hsp90 meevd peptide. Chain: g, h, i, j, k. Engineered: yes

Source:

Unidentified. Organism_taxid: 32644. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence comprises the 5 c-terminal residues of hsp90

Resolution:

2.85Å R-factor: 0.271 R-free: 0.283

Authors:

A.L.Cortajarena,J.Wang,L.Regan

Key ref:

A.L.Cortajarena et al. (2010). Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand. Febs J, 277, 1058-1066. PubMed id: 20089039

Date:

22-Oct-09 Release date: 02-Feb-10

Protein chains

No UniProt id for this chain

Struc: 102 a.a.

Febs J 277:1058-1066 (2010)

PubMed id: 20089039

Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.

A.L.Cortajarena, J.Wang, L.Regan.

ABSTRACT

Tetratricopeptide repeats (TPRs) are protein domains that mediate key protein-protein interactions in cells. Several TPR domains bind the C-termini of the chaperones heat shock protein (Hsp)90 and/or Hsp70, and exchange of such binding partners is key for the heat shock response. We have previously described the design of a TPR protein that binds tightly and specifically to the C-terminus of Hsp90, and in doing so, is able to inhibit chaperone function in vivo. Here we present the X-ray crystal structure of the designed TPR domain (CTPR390) in complex with its peptide ligand--the C-terminal residues of Hsp90 (peptide MEEVD). This structure reveals two interesting aspects of the TPR modules. First, a new packing arrangement of 3-TPR modules is observed. The TPR units stack against each other in an unusual fashion to form infinite superhelices in the crystal. Second, the structure provides insights into the molecular basis of TPR-ligand recognition.