View source for 1eqk


==SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA==
<StructureSection load='1eqk' size='340' side='right'caption='[[1eqk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eqk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
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== Function ==
[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> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eq/1eqk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eqk ConSurf].
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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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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa Japonica Group]]
[[Category: Abe K]]
[[Category: Arai S]]
[[Category: Kudo N]]
[[Category: Nagata K]]
[[Category: Tanokura M]]