1ces: Difference between revisions
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==CRYSTALS OF DEMETALLIZED CONCANAVALIN A SOAKED WITH ZINC HAVE A ZINC ION BOUND IN THE S1 SITE== | ==CRYSTALS OF DEMETALLIZED CONCANAVALIN A SOAKED WITH ZINC HAVE A ZINC ION BOUND IN THE S1 SITE== | ||
<StructureSection load='1ces' size='340' side='right' caption='[[1ces]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1ces' size='340' side='right'caption='[[1ces]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ces]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ces]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CES FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ces FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ces OCA], [https://pdbe.org/1ces PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ces RCSB], [https://www.ebi.ac.uk/pdbsum/1ces PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ces ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Concanavalin | *[[Concanavalin 3D structures|Concanavalin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Bouckaert | [[Category: Large Structures]] | ||
[[Category: Loris | [[Category: Bouckaert J]] | ||
[[Category: Poortmans | [[Category: Loris R]] | ||
[[Category: Wyns | [[Category: Poortmans F]] | ||
[[Category: Wyns L]] | |||
Latest revision as of 08:51, 9 August 2023
CRYSTALS OF DEMETALLIZED CONCANAVALIN A SOAKED WITH ZINC HAVE A ZINC ION BOUND IN THE S1 SITECRYSTALS OF DEMETALLIZED CONCANAVALIN A SOAKED WITH ZINC HAVE A ZINC ION BOUND IN THE S1 SITE
Structural highlights
FunctionCONA_CANEN D-mannose specific lectin. 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 PubMedThe lectin concanavalin A (ConA) sequentially binds a transition metal ion in the metal-binding site S1 and a calcium ion in the metal-binding site S2 to form its saccharide-binding site. Metal-free ConA crystals soaked with either Zn2+ (apoZn-ConA) or Co2+ (apoCo-ConA) display partial binding of these ions in the proto-transition metal-binding site, but no further conformational changes are observed. These structures can represent the very first step in going from metal-free ConA toward the holoprotein. In the co-crystals of metal-free ConA with Zn2+ (Zn-ConA), the zinc ion can fully occupy the S1 site. The positions of the carboxylate ligands Asp10 and Asp19 that bridge the S1 and S2 sites are affected. The ligation to Zn2+ orients Asp10 optimally for calcium ligation and stabilizes Asp19 by a hydrogen bond to one of its water ligands. The neutralizing and stabilizing effect of the binding of Zn2+ in S1 is necessary to allow for subsequent Ca2+ binding in the S2 site. However, the S2 site of monometallized ConA is still disrupted. The co-crystals of metal-free ConA with both Zn2+ and Ca2+ contain the active holoprotein (ConA ZnCa). Ca2+ has induced large conformational changes to stabilize its hepta-coordination in the S2 site, which comprise the trans to cis isomerization of the Ala207-Asp208 peptide bond accompanied by the formation of the saccharide-binding site. The Zn2+ ligation in ConA ZnCa is similar to Mn2+, Cd2+, Co2+, or Ni2+ ligation in the S1 site, in disagreement with earlier extended x-ray absorption fine structure results that suggested a lower coordination number for Zn2+. Sequential structural changes upon zinc and calcium binding to metal-free concanavalin A.,Bouckaert J, Poortmans F, Wyns L, Loris R J Biol Chem. 1996 Jul 5;271(27):16144-50. PMID:8663112[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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