1EQK
SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA
Summary for 1EQK
| Entry DOI | 10.2210/pdb1eqk/pdb |
| Descriptor | ORYZACYSTATIN-I (1 entity in total) |
| Functional Keywords | alpha and beta proteins, cystatin-like fold, cystatin/monellin superfamily, phytocystatin family, hydrolase inhibitor |
| Biological source | Oryza sativa Japonica Group |
| Cellular location | Secreted (Potential): P09229 |
| Total number of polymer chains | 1 |
| Total formula weight | 11398.89 |
| Authors | Nagata, K.,Kudo, N.,Abe, K.,Arai, S.,Tanokura, M. (deposition date: 2000-04-05, release date: 2001-01-10, Last modification date: 2024-05-22) |
| Primary citation | Nagata, K.,Kudo, N.,Abe, K.,Arai, S.,Tanokura, M. Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry, 39:14753-14760, 2000 Cited by PubMed Abstract: The three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body (Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an alpha-helix and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions (Ser2-Val12 and Ala98-Ala102) are less defined. The helix-sheet architechture of oryzacystatin-I is stabilized by a hydrophobic cluster formed between the alpha-helix and the beta-sheet and is considerably similar to that of monellin, a sweet-tasting protein from an African berry, as well as those of the animal cystatins studied, e.g., chicken egg white cystatin and human stefins A and B (also referred to as human cystatins A and B). Detailed structural comparison indicates that oryzacystatin-I is more similar to chicken cystatin, which belongs to the type-2 animal cystatins, than to human stefins A and B, which belong to the type-1 animal cystatins, despite different loop length. PubMed: 11101290DOI: 10.1021/bi0006971 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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