1HN2

CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

The insect attractant 1-octen-3-ol is the natural ligand of bovine odorant-binding protein.

Ramoni, R.Vincent, F.Grolli, S.Conti, V.Malosse, C.Boyer, F.D.Nagnan-Le Meillour, P.Spinelli, S.Cambillau, C.Tegoni, M.

(2001) J Biol Chem 276: 7150-7155

  • DOI: https://doi.org/10.1074/jbc.M010368200
  • Primary Citation of Related Structures:  
    1G85, 1HN2

  • PubMed Abstract: 

    Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.


  • Organizational Affiliation

    Architecture et Fonction des Macromolécules Biologiques, Unité Mixte de Recherche 6098, CNRS and Universités Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. vetbioc@unipr.it


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ODORANT-BINDING PROTEIN
A, B
159Bos taurusMutation(s): 0 
UniProt
Find proteins for P07435 (Bos taurus)
Explore P07435 
Go to UniProtKB:  P07435
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07435
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
ANC PDBBind:  1HN2 Kd: 1000 (nM) from 1 assay(s)
Binding MOAD:  1HN2 Kd: 1000 (nM) from 1 assay(s)
3OL Binding MOAD:  1HN2 Kd: 3300 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.589α = 90
b = 65.091β = 98.29
c = 42.249γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
CCP4data scaling
CNSphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-12-05
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2014-03-05
    Changes: Non-polymer description
  • Version 1.4: 2023-08-09
    Changes: Data collection, Database references, Derived calculations, Refinement description