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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kb0 OCA], [https://pdbe.org/5kb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kb0 RCSB], [https://www.ebi.ac.uk/pdbsum/5kb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kb0 ProSAT]</span></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=5kb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kb0 OCA], [https://pdbe.org/5kb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kb0 RCSB], [https://www.ebi.ac.uk/pdbsum/5kb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kb0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Preorganization and predisposition are important molecular recognition concepts exploited by nature to obtain site-specific and selective metal binding to proteins. While native structures containing an MS3 core are often unavailable in both apo- and holo-forms, one can use designed three-stranded coiled coils (3SCCs) containing tris-thiolate sites to evaluate these concepts. We show that the preferred metal geometry dictates the degree to which the cysteine rotamers change upon metal complexation. The Cys ligands in the apo-form are preorganized for binding trigonal pyramidal species (Pb(II)S3 and As(III)S3) in an endo conformation oriented toward the 3SCC C-termini, whereas the cysteines are predisposed for trigonal planar Hg(II)S3 and 4-coordinate Zn(II)S3O structures, requiring significant thiol rotation for metal binding. This study allows assessment of the importance of protein fold and side-chain reorientation for achieving metal selectivity in human retrotransposons and metalloregulatory proteins.
A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins.,Ruckthong L, Zastrow ML, Stuckey JA, Pecoraro VL J Am Chem Soc. 2016 Sep 2. PMID:27532255<ref>PMID:27532255</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kb0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>

Latest revision as of 13:05, 1 March 2024

Crystal Structure of a Tris-thiolate Pb(II) Complex in a de Novo Three-stranded Coiled Coil Peptide

5kb0, resolution 2.13Å

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