2kak
From Proteopedia
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| - | + | ==Solution structure of the beta-E-domain of wheat Ec-1 metallothionein== | |
| - | + | <StructureSection load='2kak' size='340' side='right' caption='[[2kak]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2kak]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KAK 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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kak OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kak RCSB], [http://www.ebi.ac.uk/pdbsum/2kak PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metallothioneins (MTs) are ubiquitous cysteine-rich proteins with a high affinity for divalent metal ions such as Zn(II), Cu(I), and Cd(II) that are involved in metal ion homeostasis and detoxification, as well as protection against reactive oxygen species. Here we show the NMR solution structure of the beta(E)-domain of the early cysteine-labeled protein (E(c)-1) from wheat (beta(E)-E(c)-1), which represents the first three-dimensional structure of a plant MT. The beta(E)-domain comprises the 51 C-terminal residues of E(c)-1 and exhibits a distinctive unprecedented structure with two separate metal-binding centers, a mononuclear Zn(II) binding site constituted by two cysteine and two highly conserved histidine residues as found in certain zinc-finger motifs, and a cluster formed by three Zn(II) ions coordinated by nine Cys residues that resembles the cluster in the beta-domain of vertebrate MTs. Cys-metal ion connectivities were determined by exhaustive structure calculations for all 7560 possible configurations of the three-metal cluster. Backbone dynamics investigated by (15)N relaxation experiments support the results of the structure determination in that beta(E)-E(c)-1 is a rigidly folded polypeptide. To further investigate the influence of metal ion binding on the stability of the structure, we replaced Zn(II) with Cd(II) ions and examined the effects of metal ion release on incubation with a metal ion chelator. | ||
| - | + | The beta(E)-domain of wheat E(c)-1 metallothionein: a metal-binding domain with a distinctive structure.,Peroza EA, Schmucki R, Guntert P, Freisinger E, Zerbe O J Mol Biol. 2009 Mar 20;387(1):207-18. Epub 2009 Jan 27. PMID:19361445<ref>PMID:19361445</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Journal:JBIC:9|Journal:JBIC:9]] | *[[Journal:JBIC:9|Journal:JBIC:9]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
| - | [[Category: Freisinger, E | + | [[Category: Freisinger, E]] |
| - | [[Category: Guntert, P | + | [[Category: Guntert, P]] |
| - | [[Category: Peroza, E A | + | [[Category: Peroza, E A]] |
| - | [[Category: Schmucki, R | + | [[Category: Schmucki, R]] |
| - | [[Category: Zerbe, O | + | [[Category: Zerbe, O]] |
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
Revision as of 14:01, 17 December 2014
Solution structure of the beta-E-domain of wheat Ec-1 metallothionein
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