1enq: Difference between revisions

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-[[Image:1enq.jpg|left|200px]]
- {{Structure
+==CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH ZINC HAVING A ZINC ION BOUND IN THE S1 SITE==
-|PDB= 1enq |SIZE=350|CAPTION= <scene name='initialview01'>1enq</scene>, resolution 2.5&Aring;
+<StructureSection load='1enq' size='340' side='right'caption='[[1enq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
+<table><tr><td colspan='2'>[[1enq]] is a 4 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=1ENQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ENQ FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<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=1enq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enq OCA], [https://pdbe.org/1enq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1enq RCSB], [https://www.ebi.ac.uk/pdbsum/1enq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1enq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
+== 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/en/1enq_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=1enq ConSurf].
+<div style="clear:both"></div>
-'''CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH ZINC HAVING A ZINC ION BOUND IN THE S1 SITE'''
+==See Also==
+*[[Concanavalin 3D structures|Concanavalin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The 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+.
-==About this Structure==
-ENQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENQ OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/8663112 8663112]
 [[Category: Canavalia ensiformis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bouckaert, J.]]
+[[Category: Bouckaert J]]
-[[Category: Loris, R.]]
+[[Category: Loris R]]
-[[Category: Poortmans, F.]]
+[[Category: Poortmans F]]
-[[Category: Wyns, L.]]
+[[Category: Wyns L]]
-[[Category: ZN]]
-[[Category: agglutinin]]
-[[Category: concanavalin some]]
-[[Category: plant lectin]]
-[[Category: zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:05 2008''