1dyt

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[[Image:1dyt.gif|left|200px]]<br />
 
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<applet load="1dyt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dyt, resolution 1.75&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE OF ECP (RNASE 3) AT 1.75 A'''<br />
 
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==Overview==
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==X-ray crystal structure of ECP (RNase 3) at 1.75 A==
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Eosinophil cationic protein (ECP; RNase 3) is a human ribonuclease found, only in eosinophil leukocytes that belongs to the RNase A superfamily., This enzyme is bactericidal, helminthotoxic and cytotoxic to mammalian, cells and tissues. The protein has been cloned, heterologously, overexpressed, purified and crystallized. Its crystal structure has been, determined and refined using data up to 1. 75 A resolution. The molecule, displays the alpha+beta folding topology typical for members of the, ribonuclease A superfamily. The catalytic active site residues are, conserved with respect to other ribonucleases of the superfamily but some, differences appear at substrate recognition subsites, which may account, in part, for the low catalytic activity. Most strikingly, 19, surface-located arginine residues confer a strong basic character to the, protein. The high concentration of positive charges and the particular, orientation of the side-chains of these residues may also be related to, the low activity of ECP as a ribonuclease and provides an explanation for, its unique cytotoxic role through cell membrane disruption.
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<StructureSection load='1dyt' size='340' side='right'caption='[[1dyt]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dyt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DYT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyt OCA], [https://pdbe.org/1dyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dyt RCSB], [https://www.ebi.ac.uk/pdbsum/1dyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dyt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECP_HUMAN ECP_HUMAN] Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.<ref>PMID:2501794</ref> <ref>PMID:19450231</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/1dyt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1dyt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Eosinophil cationic protein (ECP; RNase 3) is a human ribonuclease found only in eosinophil leukocytes that belongs to the RNase A superfamily. This enzyme is bactericidal, helminthotoxic and cytotoxic to mammalian cells and tissues. The protein has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data up to 1. 75 A resolution. The molecule displays the alpha+beta folding topology typical for members of the ribonuclease A superfamily. The catalytic active site residues are conserved with respect to other ribonucleases of the superfamily but some differences appear at substrate recognition subsites, which may account, in part, for the low catalytic activity. Most strikingly, 19 surface-located arginine residues confer a strong basic character to the protein. The high concentration of positive charges and the particular orientation of the side-chains of these residues may also be related to the low activity of ECP as a ribonuclease and provides an explanation for its unique cytotoxic role through cell membrane disruption.
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==About this Structure==
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Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution.,Mallorqui-Fernandez G, Pous J, Peracaula R, Aymami J, Maeda T, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M J Mol Biol. 2000 Jul 28;300(5):1297-307. PMID:10903870<ref>PMID:10903870</ref>
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1DYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FE and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: ASA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DYT OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution., Mallorqui-Fernandez G, Pous J, Peracaula R, Aymami J, Maeda T, Tada H, Yamada H, Seno M, de Llorens R, Gomis-Ruth FX, Coll M, J Mol Biol. 2000 Jul 28;300(5):1297-307. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903870 10903870]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1dyt" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Coll, M.]]
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[[Category: Gomis-Rueth, F.X.]]
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[[Category: Llorens, R.De.]]
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[[Category: Maeda, T.]]
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[[Category: Mallorqui-Fernandez, G.]]
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[[Category: Peracaula, R.]]
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[[Category: Pous, J.]]
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[[Category: Seno, M.]]
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[[Category: Tada, H.]]
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[[Category: Yamada, H.]]
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[[Category: CIT]]
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[[Category: FE]]
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[[Category: ecp]]
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[[Category: eosinophil cationic protein]]
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[[Category: rnase 3]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:02:38 2007''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Coll M]]
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[[Category: De Llorens R]]
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[[Category: Gomis-Rueth FX]]
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[[Category: Maeda T]]
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[[Category: Mallorqui-Fernandez G]]
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[[Category: Peracaula R]]
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[[Category: Pous J]]
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[[Category: Seno M]]
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[[Category: Tada H]]
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[[Category: Yamada H]]

Current revision

X-ray crystal structure of ECP (RNase 3) at 1.75 A

PDB ID 1dyt

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