1RIE

STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX

PDB DOI: https://doi.org/10.2210/pdb1RIE/pdb

Classification: ELECTRON TRANSPORT
Organism(s): Bos taurus
Mutation(s): No

Deposited: 1996-02-23 Released: 1996-12-07
Deposition Author(s): Iwata, S., Saynovits, M., Link, T.A., Michel, H.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.211
R-Value Work: 0.187
R-Value Observed: 0.187

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.

Iwata, S., Saynovits, M., Link, T.A., Michel, H.

(1996) Structure 4: 567-579

PubMed: 8736555 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(96)00062-7
Primary Citation of Related Structures:
1RIE

PubMed Abstract:
The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies.

Organizational Affiliation

Max-Planck-Institut für Biophysik, Abt. Molekulare Membranbiologie, Frankfurt/Main., Germany.

Macromolecule Content

Total Structure Weight: 14.62 kDa
Atom Count: 1,169
Modelled Residue Count: 127
Deposited Residue Count: 129
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
RIESKE IRON-SULFUR PROTEIN	A	129	Bos taurus	Mutation(s): 0 EC: 1.10.2.2
UniProt
Find proteins for P13272 (Bos taurus) Explore P13272 Go to UniProtKB: P13272
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P13272
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FES Query on FES Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	FE2/S2 (INORGANIC) CLUSTER Fe₂ S₂ NIXDOXVAJZFRNF-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.211
R-Value Work: 0.187
R-Value Observed: 0.187
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 32.1	α = 90
b = 53	β = 100.3
c = 38	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
MLPHARE	phasing
X-PLOR	refinement

Structure Validation

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Entry History

Deposition Data

Released Date: 1996-12-07

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1996-12-07
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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.