1HF9

C-Terminal Coiled-Coil Domain from Bovine IF1


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 35 
  • Selection Criteria: LOWEST ENERGIES 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.

Gordon-Smith, D.J.Carbajo, R.J.Yang, J.C.Videler, H.Runswick, M.J.Walker, J.E.Neuhaus, D.

(2001) J Mol Biol 308: 325-339

  • DOI: https://doi.org/10.1006/jmbi.2001.4570
  • Primary Citation of Related Structures:  
    1HF9

  • PubMed Abstract: 

    Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.


  • Organizational Affiliation

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATPASE INHIBITOR (MITOCHONDRIAL)
A, B
41Bos taurusMutation(s): 0 
UniProt
Find proteins for P01096 (Bos taurus)
Explore P01096 
Go to UniProtKB:  P01096
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01096
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 35 
  • Selection Criteria: LOWEST ENERGIES 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-05-31
    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: 2018-01-17
    Changes: Database references
  • Version 1.4: 2020-01-15
    Changes: Data collection, Other
  • Version 1.5: 2024-05-15
    Changes: Data collection, Database references