View source for 6egl


==Crystal Structure of a de Novo Three-stranded Coiled Coil Peptide Containing a D-Leu in the Second Coordination Sphere of a Non-metalated Tris-thiolate Binding Site==
<StructureSection load='6egl' size='340' side='right'caption='[[6egl]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6egl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EGL 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</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=6egl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6egl OCA], [https://pdbe.org/6egl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6egl RCSB], [https://www.ebi.ac.uk/pdbsum/6egl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6egl ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6egl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Pecoraro VL]]
[[Category: Ruckthong L]]
[[Category: Stuckey JA]]