2BRZ
SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE
Summary for 2BRZ
| Entry DOI | 10.2210/pdb2brz/pdb |
| Descriptor | BRAZZEIN (1 entity in total) |
| Functional Keywords | sweet protein, cysteine-stabilized alpha-beta |
| Biological source | Pentadiplandra brazzeana |
| Total number of polymer chains | 1 |
| Total formula weight | 6491.33 |
| Authors | Caldwell, J.E.,Abildgaard, F.,Dzakula, Z.,Ming, D.,Hellekant, G.,Markley, J.L. (deposition date: 1998-04-30, release date: 1998-07-01, Last modification date: 2024-11-20) |
| Primary citation | Caldwell, J.E.,Abildgaard, F.,Dzakula, Z.,Ming, D.,Hellekant, G.,Markley, J.L. Solution structure of the thermostable sweet-tasting protein brazzein. Nat.Struct.Biol., 5:427-431, 1998 Cited by 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. PubMed: 9628478DOI: 10.1038/nsb0698-427 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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