2nu5
From Proteopedia
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| - | [[Image:2nu5.jpg|left|200px]] | ||
| - | + | ==Crystal structure of a complex of griffithsin cocrystallized with N-acetylglucosamine== | |
| - | + | <StructureSection load='2nu5' size='340' side='right'caption='[[2nu5]], [[Resolution|resolution]] 1.56Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[2nu5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Griffithsia_sp._Q66D336 Griffithsia sp. Q66D336]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NU5 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]] 1.564Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2nu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nu5 OCA], [https://pdbe.org/2nu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nu5 RCSB], [https://www.ebi.ac.uk/pdbsum/2nu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nu5 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/GRFIN_GRISQ GRFIN_GRISQ] | |
| - | + | == 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/nu/2nu5_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=2nu5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes. | Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes. | ||
| - | + | Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine.,Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A Protein Sci. 2007 Jul;16(7):1485-9. Epub 2007 Jun 13. PMID:17567736<ref>PMID:17567736</ref> | |
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| - | Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine., Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2nu5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Griffithsia sp. Q66D336]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wlodawer A]] | ||
| + | [[Category: Ziolkowska NE]] | ||
Current revision
Crystal structure of a complex of griffithsin cocrystallized with N-acetylglucosamine
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