2BRZ

SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 
  • Conformers Submitted: 
  • Selection Criteria: MINIMIZED AVERAGE 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Solution structure of the thermostable sweet-tasting protein brazzein.

Caldwell, J.E.Abildgaard, F.Dzakula, Z.Ming, D.Hellekant, G.Markley, J.L.

(1998) Nat Struct Biol 5: 427-431

  • DOI: https://doi.org/10.1038/nsb0698-427
  • Primary Citation of Related Structures:  
    1BRZ, 2BRZ

  • PubMed Abstract: 

    The fruit of Pentadiplandra brazzeana Baillon contains a small, sweet-tasting protein named brazzein. The structure of brazzein in solution was determined by proton nuclear magnetic resonance spectroscopy at pH 5.2 and 22 degrees C. The brazzein fold, which contains one alpha-helix and three strands of antiparallel beta-sheet, does not resemble that of either of the other two sweet-tasting proteins with known structures, monellin and thaumatin. Instead, the structure of brazzein resembles those of plant gamma-thionins and defensins and arthropod toxins. Sequence comparisons predict that members of a newly-identified family of serine proteinase inhibitors share the brazzein fold.


  • Organizational Affiliation

    Graduate Program in Biophysics, University of Wisconsin-Madison 53706, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BRAZZEIN54Pentadiplandra brazzeanaMutation(s): 0 
UniProt
Find proteins for P56552 (Pentadiplandra brazzeana)
Explore P56552 
Go to UniProtKB:  P56552
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56552
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
PCA
Query on PCA
A
L-PEPTIDE LINKINGC5 H7 N O3GLN
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 
  • Conformers Submitted: 
  • Selection Criteria: MINIMIZED AVERAGE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-07-01
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2019-12-25
    Changes: Derived calculations, Other, Polymer sequence