1GMJ

The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase

PDB DOI: https://doi.org/10.2210/pdb1GMJ/pdb

Classification: ATPASE INHIBITOR
Organism(s): Bos taurus
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2001-09-14 Released: 2002-01-01
Deposition Author(s): Cabezon, E., Runswick, M.J., Leslie, A.G.W., Walker, J.E.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.280
R-Value Work: 0.258
R-Value Observed: 0.258

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

The Structure of Bovine If(1), the Regulatory Subunit of Mitochondrial F-ATPase.

Cabezon, E., Runswick, M.J., Leslie, A.G.W., Walker, J.E.

(2001) EMBO J 20: 6990

PubMed: 11742976 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1093/emboj/20.24.6990
Primary Citation of Related Structures:
1GMJ

PubMed Abstract:
In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase.

Organizational Affiliation

The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.

Macromolecule Content

Total Structure Weight: 38.38 kDa
Atom Count: 2,037
Modelled Residue Count: 240
Deposited Residue Count: 336
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ATPASE INHIBITOR	A, B, C, D	84	Bos taurus	Mutation(s): 0
UniProt
Find proteins for P01096 (Bos taurus) Explore P01096 Go to UniProtKB: P01096
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P01096
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.280
R-Value Work: 0.258
R-Value Observed: 0.258
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 32.01	α = 90
b = 53.29	β = 95.89
c = 156.94	γ = 90

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2002-01-01

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2002-01-01
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2018-01-24
Changes: Source and taxonomy
Version 1.4: 2019-05-15
Changes: Data collection, Experimental preparation

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.