1lq7: Difference between revisions

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{{Seed}}
[[Image:1lq7.png|left|200px]]


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==De Novo Designed Protein Model of Radical Enzymes==
The line below this paragraph, containing "STRUCTURE_1lq7", creates the "Structure Box" on the page.
<StructureSection load='1lq7' size='340' side='right'caption='[[1lq7]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=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>
{{STRUCTURE_1lq7|  PDB=1lq7  |  SCENE=  }}
</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.


===De Novo Designed Protein Model of Radical Enzymes===
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>
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The line below this paragraph, {{ABSTRACT_PUBMED_12224922}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1lq7" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 12224922 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12224922}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ7 OCA].
[[Category: Blomberg M]]
 
[[Category: Dai Q-H]]
==Reference==
[[Category: Dutton PL]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12224922 12224922]
[[Category: Fuentes EJ]]
[[Category: Blomberg, M.]]
[[Category: Tommos C]]
[[Category: Dai, Q H.]]
[[Category: Wand AJ]]
[[Category: Dutton, P L.]]
[[Category: Fuentes, E J.]]
[[Category: Tommos, C.]]
[[Category: Wand, A J.]]
[[Category: Three helix bundle]]
 
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