1GUR
GURMARIN, A SWEET TASTE-SUPPRESSING POLYPEPTIDE, NMR, 10 STRUCTURES
Summary for 1GUR
| Entry DOI | 10.2210/pdb1gur/pdb |
| Descriptor | GURMARIN (1 entity in total) |
| Functional Keywords | sweet-taste, suppressing protein, sweet taste-suppressing protein |
| Biological source | Gymnema sylvestre |
| Total number of polymer chains | 1 |
| Total formula weight | 4220.95 |
| Authors | Arai, K.,Ishima, R.,Morikawa, S.,Imoto, T.,Yoshimura, S.,Aimoto, S.,Akasaka, K. (deposition date: 1996-03-12, release date: 1996-08-01, Last modification date: 2024-10-23) |
| Primary citation | Arai, K.,Ishima, R.,Morikawa, S.,Miyasaka, A.,Imoto, T.,Yoshimura, S.,Aimoto, S.,Akasaka, K. Three-dimensional structure of gurmarin, a sweet taste-suppressing polypeptide. J.Biomol.NMR, 5:297-305, 1995 Cited by PubMed Abstract: The solution structure of gurmarin was studied by two-dimensional proton NMR spectroscopy at 600 MHz. Gurmarin, a 35-amino acid residue polypeptide recently discovered in an Indian-originated tree Gymnema sylvestre, selectively suppresses the neural responses of rat to sweet taste stimuli. Sequence-specific resonance assignments were obtained for all backbone protons and for most of the side-chain protons. The three-dimensional solution structure was determined by simulated-annealing calculations on the basis of 135 interproton distance constraints derived from NOEs, six distance constraints for three hydrogen bonds and 16 dihedral angle constraints derived from coupling constants. A total of 10 structures folded into a well-defined structure with a triple-stranded antiparallel beta-sheet. The average rmsd values between any two structures were 1.65 +/- 0.39 A for the backbone atoms (N, C alpha, C) and 2.95 +/- 0.27 A for all heavy atoms. The positions of the three disulfide bridges, which could not be determined chemically, were estimated to be Cys3-Cys18, Cys10-Cys23 and Cys17-Cys33 on the basis of the NMR distance constraints. This disulfide bridge pattern in gurmarin turned out to be analogous to that in omega-conotoxin and Momordica charantia trypsin inhibitor-II, and the topology of folding was the same as that in omega-conotoxin. PubMed: 7787425DOI: 10.1007/BF00211756 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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