View source for 1lq7


==De Novo Designed Protein Model of Radical Enzymes==
<StructureSection load='1lq7' size='340' side='right'caption='[[1lq7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lq7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQ7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lq7 OCA], [https://pdbe.org/1lq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lq7 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The use of side chains as catalytic cofactors for protein mediated redox chemistry raises significant mechanistic issues as to how these amino acids are activated toward radical chemistry in a controlled manner. De novo protein design has been used to examine the structural basis for the creation and maintenance of a tryptophanyl radical in a three-helix bundle protein maquette. Here we report the detailed structural analysis of the protein by multidimensional NMR methods. An interesting feature of the structure is an apparent pi-cation interaction involving the sole tryptophan and a lysine side chain. Hybrid density functional calculations support the notion that this interaction raises the reduction potential of the W degrees /WH redox pair and helps explain the redox characteristics of the protein. This model protein system therefore provides a powerful model for exploring the structural basis for controlled radical chemistry in protein.

Structure of a de novo designed protein model of radical enzymes.,Dai QH, Tommos C, Fuentes EJ, Blomberg MR, Dutton PL, Wand AJ J Am Chem Soc. 2002 Sep 18;124(37):10952-3. PMID:12224922<ref>PMID:12224922</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lq7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Blomberg M]]
[[Category: Dai Q-H]]
[[Category: Dutton PL]]
[[Category: Fuentes EJ]]
[[Category: Tommos C]]
[[Category: Wand AJ]]