This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3enr
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3enr.png|left|200px]] | ||
| - | + | ==ZINC-CALCIUM CONCANAVALIN A AT PH 6.15== | |
| + | <StructureSection load='3enr' size='340' side='right'caption='[[3enr]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3enr]] 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=3ENR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ENR 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]] 2.4Å</td></tr> | ||
| + | <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=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=3enr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3enr OCA], [https://pdbe.org/3enr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3enr RCSB], [https://www.ebi.ac.uk/pdbsum/3enr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3enr 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/3enr_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=3enr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structures of cadmium/cadmium and zinc/calcium concanavalin A (con A) at pH 5.0 and pH 6.15, respectively, were determined. The structure of cadmium/cadmium con A confirms that the secondary Cd(2+)-binding site S3 is empty at pH 5. The metal-binding sites S1 and S2 are only very slightly affected by the substitution with cadmium. On the other hand, S1 and S2 and most of the protein surface of zinc/calcium con A at pH 6.15 differ from other fully metal-bound and carbohydrate-free structures. Most of these structural differences at the protein surface are a result of the interplay between metal binding, protonation and crystal packing. This interplay is expressed by relative rotations and translations of the con A units in alternative crystal packings and participation in space-group conversions inside crystals in situ. The particular crystal packing of zinc/calcium con A creates a novel zinc-binding site S4. The Zn(2+) ion in S4 ligates two aspartates from one tetramer and a histidine from a symmetry-related tetramer. | ||
| - | + | Zinc/calcium- and cadmium/cadmium-substituted concanavalin A: interplay of metal binding, pH and molecular packing.,Bouckaert J, Loris R, Wyns L Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1569-76. PMID:11092923<ref>PMID:11092923</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3enr" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Concanavalin | + | *[[Concanavalin 3D structures|Concanavalin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Bouckaert J]] |
| - | [[Category: | + | [[Category: Loris R]] |
| - | [[Category: | + | [[Category: Wyns L]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
ZINC-CALCIUM CONCANAVALIN A AT PH 6.15
| |||||||||||

