2kb5: Difference between revisions
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==Solution NMR Structure of Eosinophil Cationic Protein/RNase 3== | |||
<StructureSection load='2kb5' size='340' side='right'caption='[[2kb5]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kb5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KB5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2kb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kb5 OCA], [https://pdbe.org/2kb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2kb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kb5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
== 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/kb/2kb5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2kb5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eosinophil cationic protein (ECP) / human RNase 3, a member of the RNase A family, is a remarkably cytotoxic protein implicated in asthma and allergies. These activites are probably due to ECP's ability to interact with and disrupt membranes and depend on two Trp, 19 Arg and possibly an extremely high conformational stability. Here, we have used NMR spectroscopy to assign essentially all (1)H, (15)N and backbone (13)C resonances, to solve the 3D structure in aqueous solution and to quantify its residue-level stability. The NMR solution structure was determined on the basis of 2316 distance constraints and is well-defined (backbone RMSD = 0.75A). The N-terminus and the loop composed of residues 114-123 are relatively well-ordered; in contrast, conformational diversity is observed for the loop segments 17-22, 65-68 and 92-95 and most exposed sidechains. The side chain NH groups of the two Trp and 19 Arg showed no significant protection against hydrogen/deuterium exchange. The most protected NH groups belong to the first and last two square-strands, and curiously, the first square-helix. Analysis of their exchange rates reveals a strikingly high global stability of 11.8 kcal/mol. This value and other stability measurements are used to better quantify ECP's unfolding thermodynamics. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009. | |||
"The (1)H, (13)C, (15)N resonance assignment, solution structure and residue level stability of eosinophil cationic protein/rnase 3 determined by NMR spectroscopy",Laurents DV, Bruix M, Jimenez MA, Santoro J, Boix E, Moussaoui M, Nogues MV, Rico M Biopolymers. 2009 Feb 2. PMID:19189375<ref>PMID:19189375</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kb5" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Boix | [[Category: Large Structures]] | ||
[[Category: Bruix | [[Category: Boix E]] | ||
[[Category: Jimenez | [[Category: Bruix M]] | ||
[[Category: Laurents | [[Category: Jimenez M]] | ||
[[Category: Moussaoui | [[Category: Laurents DV]] | ||
[[Category: Nogues | [[Category: Moussaoui M]] | ||
[[Category: Rico | [[Category: Nogues M]] | ||
[[Category: Santoro | [[Category: Rico M]] | ||
[[Category: Santoro J]] | |||
Latest revision as of 12:14, 6 November 2024
Solution NMR Structure of Eosinophil Cationic Protein/RNase 3Solution NMR Structure of Eosinophil Cationic Protein/RNase 3
Structural highlights
FunctionECP_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.[1] [2] 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 PubMedEosinophil cationic protein (ECP) / human RNase 3, a member of the RNase A family, is a remarkably cytotoxic protein implicated in asthma and allergies. These activites are probably due to ECP's ability to interact with and disrupt membranes and depend on two Trp, 19 Arg and possibly an extremely high conformational stability. Here, we have used NMR spectroscopy to assign essentially all (1)H, (15)N and backbone (13)C resonances, to solve the 3D structure in aqueous solution and to quantify its residue-level stability. The NMR solution structure was determined on the basis of 2316 distance constraints and is well-defined (backbone RMSD = 0.75A). The N-terminus and the loop composed of residues 114-123 are relatively well-ordered; in contrast, conformational diversity is observed for the loop segments 17-22, 65-68 and 92-95 and most exposed sidechains. The side chain NH groups of the two Trp and 19 Arg showed no significant protection against hydrogen/deuterium exchange. The most protected NH groups belong to the first and last two square-strands, and curiously, the first square-helix. Analysis of their exchange rates reveals a strikingly high global stability of 11.8 kcal/mol. This value and other stability measurements are used to better quantify ECP's unfolding thermodynamics. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009. "The (1)H, (13)C, (15)N resonance assignment, solution structure and residue level stability of eosinophil cationic protein/rnase 3 determined by NMR spectroscopy",Laurents DV, Bruix M, Jimenez MA, Santoro J, Boix E, Moussaoui M, Nogues MV, Rico M Biopolymers. 2009 Feb 2. PMID:19189375[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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