PDBsum entry 2f4e

Signaling protein

PDB id: 2f4e

Contents

Protein chains

131 a.a. *

Waters ×46

* Residue conservation analysis

PDB id:

2f4e

Name:

Signaling protein

Title:

N-terminal domain of fkbp42 from arabidopsis thaliana

Structure:

Atfkbp42. Chain: a, b. Fragment: n-terminal fkbp-type domain, residues 1-180. Synonym: twd1 (twisted dwarf 1). Engineered: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Strain: ecotype columbia. Gene: twd1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Dimer (from PQS)

Resolution:

2.32Å R-factor: 0.246 R-free: 0.283

Authors:

O.H.Weiergraber,A.Eckhoff,J.Granzin

Key ref:

O.H.Weiergräber et al. (2006). Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters. FEBS Lett, 580, 251-255. PubMed id: 16364310 DOI: 10.1016/j.febslet.2005.12.007

Date:

23-Nov-05 Release date: 10-Jan-06

Protein chains

Q9LDC0  (FKB42_ARATH) -  Peptidyl-prolyl cis-trans isomerase FKBP42 from Arabidopsis thaliana

Seq: 365 a.a.

Struc: 131 a.a.

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

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

Added reference

DOI no: 10.1016/j.febslet.2005.12.007

FEBS Lett 580:251-255 (2006)

PubMed id: 16364310

Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters.

O.H.Weiergräber, A.Eckhoff, J.Granzin.

ABSTRACT

We present the three-dimensional structure of the N-terminal FK506-binding protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana. The data provide the structural background for the explanation of key functional properties reported previously.

Selected figure(s)

Figure 1.
Fig. 1. Superposition of the crystal structures of AtFKBP42^1-180 (blue), HsFKBP12 (grey) and AtFKBP13 (orange). Secondary structure elements of the canonical FKBP fold are numbered consecutively; β0 is an additional β-strand present in AtFKBP42^1-180. The FK506 molecule bound to HsFKBP12 is shown as stick model.

Figure 3.
Fig. 3. Comparison of the molecular surfaces of HsFKBP12 (A) and AtFKBP42^1-180 (B). The FK506 ligand (dark grey) is positioned as in the complex with HsFKBP12. Orientation of the molecules is the same as in Fig. 2.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2006, 580, 251-255) copyright 2006.

Figures were selected by the author.