2gn7
From Proteopedia
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| - | [[Image:2gn7.gif|left|200px]]<br /><applet load="2gn7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2gn7, resolution 2.90Å" /> | ||
| - | '''Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-3)Man-alpha(1-6)Man'''<br /> | ||
| - | == | + | ==Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-3)Man-alpha(1-6)Man== |
| + | <StructureSection load='2gn7' size='340' side='right'caption='[[2gn7]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2gn7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pterocarpus_angolensis Pterocarpus angolensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GN7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ukg|1ukg]], [[2gme|2gme]], [[2gmm|2gmm]], [[2gnm|2gnm]], [[2gmp|2gmp]], [[2gn3|2gn3]], [[2gnb|2gnb]], [[2gnd|2gnd]], [[2gnt|2gnt]]</div></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=2gn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gn7 OCA], [https://pdbe.org/2gn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2gn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gn7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/gn/2gn7_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=2gn7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype. | The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype. | ||
| - | + | Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.,Garcia-Pino A, Buts L, Wyns L, Loris R J Mol Biol. 2006 Aug 4;361(1):153-67. Epub 2006 Jun 21. PMID:16824540<ref>PMID:16824540</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2gn7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pterocarpus angolensis]] | [[Category: Pterocarpus angolensis]] | ||
| - | + | [[Category: Buts, L]] | |
| - | [[Category: Buts, L | + | [[Category: Garcia-Pino, A]] |
| - | [[Category: Garcia-Pino, A | + | [[Category: Loris, R]] |
| - | [[Category: Loris, R | + | [[Category: Wyns, L]] |
| - | [[Category: Wyns, L | + | [[Category: Beta sandwich]] |
| - | [[Category: | + | [[Category: Legume lectin]] |
| - | + | [[Category: Metal-free lectin]] | |
| - | [[Category: | + | [[Category: Sugar binding protein]] |
| - | [[Category: | + | [[Category: Sugar complex]] |
| - | [[Category: | + | |
| - | [[Category: | + | |
| - | + | ||
| - | + | ||
Current revision
Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-3)Man-alpha(1-6)Man
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