Structural highlights
Function
CYT1_ORYSJ There are two distinct cystatins in rice seeds (Oryzacystatin-1 and -2) with different specificities against cysteine proteinases. May be involved in the control of germination by inhibition of endogenous cysteine proteinases. May play a role in defense by inhibiting exogenous proteases such as those present in digestive tracks of insects and nematodes.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.,Nagata K, Kudo N, Abe K, Arai S, Tanokura M Biochemistry. 2000 Dec 5;39(48):14753-60. PMID:11101290[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kondo H, Abe K, Nishimura I, Watanabe H, Emori Y, Arai S. Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II. J Biol Chem. 1990 Sep 15;265(26):15832-7. PMID:1697595
- ↑ 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. 2000 Dec 5;39(48):14753-60. PMID:11101290
