2gnt

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[[Image:2gnt.gif|left|200px]]
 
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{{Structure
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==EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)==
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|PDB= 2gnt |SIZE=350|CAPTION= <scene name='initialview01'>2gnt</scene>, resolution 2.02&Aring;
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<StructureSection load='2gnt' size='340' side='right'caption='[[2gnt]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[2gnt]] 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=2GNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GNT FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.02&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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}}
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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=2gnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gnt OCA], [https://pdbe.org/2gnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gnt RCSB], [https://www.ebi.ac.uk/pdbsum/2gnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gnt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8GSD2_PTEAG Q8GSD2_PTEAG]
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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/gn/2gnt_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=2gnt 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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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.
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'''EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2gnt" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Pal|Pal]]
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== References ==
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==About this Structure==
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<references/>
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2GNT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pterocarpus_angolensis Pterocarpus angolensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GNT OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16824540 16824540]
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[[Category: Pterocarpus angolensis]]
[[Category: Pterocarpus angolensis]]
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[[Category: Single protein]]
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[[Category: Buts L]]
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[[Category: Buts, L.]]
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[[Category: Garcia-Pino A]]
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[[Category: Garcia-Pino, A.]]
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[[Category: Loris R]]
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[[Category: Loris, R.]]
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[[Category: Wyns L]]
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[[Category: Wyns, L.]]
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[[Category: CA]]
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[[Category: beta sandwich]]
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[[Category: legume lectin]]
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[[Category: metal binding]]
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[[Category: pal]]
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[[Category: remetallization]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:06:58 2008''
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Current revision

EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)

PDB ID 2gnt

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OCA

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