2IF4

Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana

PDB DOI: https://doi.org/10.2210/pdb2IF4/pdb

Classification: SIGNALING PROTEIN
Organism(s): Arabidopsis thaliana
Expression System: Escherichia coli BL21
Mutation(s): No

Deposited: 2006-09-20 Released: 2006-10-31
Deposition Author(s): Granzin, J., Eckhoff, A., Weiergraeber, O.H.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.85 Å
R-Value Free: 0.355
R-Value Work: 0.290
R-Value Observed: 0.296

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal Structure of a Multi-domain Immunophilin from Arabidopsis thaliana: A Paradigm for Regulation of Plant ABC Transporters.

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

(2006) J Mol Biol 364: 799-809

PubMed: 17045295 Search on PubMed
DOI: https://doi.org/10.1016/j.jmb.2006.09.052
Primary Citation of Related Structures:
2IF4

PubMed Abstract:
FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.

Organizational Affiliation

Institute of Neurosciences and Biophysics, Molecular Biophysics, Research Centre Jülich, D-52425 Jülich, Germany.

Macromolecule Content

Total Structure Weight: 38.36 kDa
Atom Count: 2,072
Modelled Residue Count: 258
Deposited Residue Count: 338
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ATFKBP42	A	338	Arabidopsis thaliana	Mutation(s): 0 Gene Names: FKBP42, TWD1, UCU2
UniProt
Find proteins for Q9LDC0 (Arabidopsis thaliana) Explore Q9LDC0 Go to UniProtKB: Q9LDC0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9LDC0
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.85 Å
R-Value Free: 0.355
R-Value Work: 0.290
R-Value Observed: 0.296
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 86.142	α = 90
b = 117.873	β = 90
c = 40.112	γ = 90

Software Package:

Software Name	Purpose
MLPHARE	phasing
CNS	refinement
MOSFLM	data reduction
CCP4	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2006-10-31

Deposition Author(s):

Weiergraeber, O.H.

Revision History (Full details and data files)

Version 1.0: 2006-10-31
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-21
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.