1eqk

<StructureSection load='1eqk' size='340' side='right'caption='[[1eqk]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1eqk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQK FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqk OCA], [https://pdbe.org/1eqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eqk RCSB], [https://www.ebi.ac.uk/pdbsum/1eqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eqk ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CYT1_ORYSJ 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.<ref>PMID:1697595</ref>

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== 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<ref>PMID:11101290</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1eqk" style="background-color:#fffaf0;"></div>

[[Category: Japanese rice]]

[[Category: Abe, K]]

[[Category: Arai, S]]

[[Category: Kudo, N]]

[[Category: Nagata, K]]

[[Category: Tanokura, M]]

[[Category: Phytocystatin family]]