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3e85
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Pathogenesis-related Protein LlPR-10.2B from yellow lupine in complex with Diphenylurea== | |
| + | <StructureSection load='3e85' size='340' side='right'caption='[[3e85]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3e85]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E85 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSU:1,3-DIPHENYLUREA'>BSU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3e85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e85 OCA], [https://pdbe.org/3e85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e85 RCSB], [https://www.ebi.ac.uk/pdbsum/3e85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e85 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P102B_LUPLU P102B_LUPLU] Class II ribonuclease (RNase) (By similarity). Binds to several cytokinins including natural adenine-type (e.g. trans-zeatin and kinetin) and artificial urea-type (e.g. N,N'-diphenylurea and N-phenyl-N'-(2-chloro-4-pyridyl)urea) hormones (PubMed:18406424, PubMed:19220853, PubMed:29630775). Interacts with melatonin (PubMed:29630775).[UniProtKB:P52779]<ref>PMID:18406424</ref> <ref>PMID:19220853</ref> <ref>PMID:29630775</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/e8/3e85_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=3e85 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plant pathogenesis-related (PR) proteins of class 10 are the only group among the 17 PR protein families that are intracellular and cytosolic. Sequence conservation and the wide distribution of PR-10 proteins throughout the plant kingdom are an indication of an indispensable function in plants, but their true biological role remains obscure. Crystal and solution structures for several homologues have shown a similar overall fold with a vast internal cavity which, together with structural similarities to the steroidogenic acute regulatory protein-related lipid transfer domain and cytokinin-specific binding proteins, strongly indicate a ligand-binding role for the PR-10 proteins. This article describes the structure of a complex between a classic PR-10 protein [Lupinus luteus (yellow lupine) PR-10 protein of subclass 2, LlPR-10.2B] and N,N'-diphenylurea, a synthetic cytokinin. Synthetic cytokinins have been shown in various bioassays to exhibit activity similar to that of natural cytokinins. The present 1.95 A resolution crystallographic model reveals four N,N'-diphenylurea molecules in the hydrophobic cavity of the protein and a degree of conformational changes accompanying ligand binding. The structural adaptability of LlPR-10.2B and its ability to bind different cytokinins suggest that this protein, and perhaps other PR-10 proteins as well, can act as a reservoir of cytokinin molecules in the aqueous environment of a plant cell. | ||
| - | + | Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein.,Fernandes H, Bujacz A, Bujacz G, Jelen F, Jasinski M, Kachlicki P, Otlewski J, Sikorski MM, Jaskolski M FEBS J. 2009 Mar;276(6):1596-609. Epub 2009 Feb 11. PMID:19220853<ref>PMID:19220853</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3e85" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lupinus luteus]] | ||
| + | [[Category: Bujacz A]] | ||
| + | [[Category: Bujacz G]] | ||
| + | [[Category: Fernandes HC]] | ||
| + | [[Category: Jaskolski M]] | ||
| + | [[Category: Sikorski MM]] | ||
Current revision
Crystal Structure of Pathogenesis-related Protein LlPR-10.2B from yellow lupine in complex with Diphenylurea
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