6ego: Difference between revisions
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==Crystal Structure of a de Novo Three-stranded Coiled Coil Peptide Containing an Ala Residue in the Second Coordination Sphere of the Hg(II)S3 Binding Site== | |||
<StructureSection load='6ego' size='340' side='right'caption='[[6ego]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ego]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EGO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ego FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ego OCA], [http://pdbe.org/6ego PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ego RCSB], [http://www.ebi.ac.uk/pdbsum/6ego PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ego ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A challenging objective of De Novo metalloprotein design is to control of the second coordination sphere of an active site to fine tune metal properties.The well-defined three stranded coiled coils, TRI and CoilSer peptides, are used to address this question.Substitution of Cys for Leu yields a thiophilic site within the core. Metals such as Hg(II), Pb(II) and As(III) result in trigonal planar or trigonal pyramidal geometries; however, spectroscopic studies showed Cd(II) formed 3-, 4- or 5-coordinate Cd(II)S(3)(OH(2))x (where x=0-2) when the second coordination sphere was perturbed.Unfortunately, there has been little crystallographic examination of these proteins to explain the observations.Herein,we compare the high-resolution x-ray structures of apo- and mercurated proteins to explain the modifications that lead to metal coordination number and geometry variation.It reveals that Ala substitution for Leu opens a cavity above the Cys site allowing for water excess, facilitating Cd(II)S(3)(OH(2)).Replacement of Cys by Pen restricts thiol rotation, causing a shift in the metal binding plane that displaces water, forming Cd(II)S(3).D-Leu, above the Cys site, reorients the side chain towards the Cys layer diminishing the space for water accommodation yielding Cd(II)S(3), while D-Leu below opens more space, allowing for equal Cd(II)S(3)(OH(2)) and Cd(II)S(3)(OH(2))(2).These studies provide insights on how to control desired metal geometries in metalloproteins using coded and non-coded amino acids. | |||
How Second Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.,Pecoraro VL, Ruckthong L, Stuckey JA Chemistry. 2019 Mar 12. doi: 10.1002/chem.201806040. PMID:30861211<ref>PMID:30861211</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ego" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pecoraro, V L]] | |||
[[Category: Ruckthong, L]] | [[Category: Ruckthong, L]] | ||
[[Category: | [[Category: Stuckey, J A]] | ||
[[Category: De novo protein]] | |||
[[Category: De novo three-stranded helical coiled coil peptide]] | |||
