1lq7

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[[Image:1lq7.jpg|left|200px]]
 
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==De Novo Designed Protein Model of Radical Enzymes==
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The line below this paragraph, containing "STRUCTURE_1lq7", creates the "Structure Box" on the page.
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<StructureSection load='1lq7' size='340' side='right'caption='[[1lq7]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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{{STRUCTURE_1lq7| PDB=1lq7 | SCENE= }}
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</table>
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<div style="background-color:#fffaf0;">
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'''De Novo Designed Protein Model of Radical Enzymes'''
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== Publication Abstract from PubMed ==
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==Overview==
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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.
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.
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==About this Structure==
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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>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Blomberg, M.]]
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<div class="pdbe-citations 1lq7" style="background-color:#fffaf0;"></div>
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[[Category: Dai, Q H.]]
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== References ==
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[[Category: Dutton, P L.]]
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<references/>
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[[Category: Fuentes, E J.]]
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__TOC__
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[[Category: Tommos, C.]]
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</StructureSection>
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[[Category: Wand, A J.]]
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[[Category: Large Structures]]
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[[Category: Three helix bundle]]
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[[Category: Blomberg M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:10:08 2008''
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[[Category: Dai Q-H]]
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[[Category: Dutton PL]]
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[[Category: Fuentes EJ]]
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[[Category: Tommos C]]
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[[Category: Wand AJ]]

Current revision

De Novo Designed Protein Model of Radical Enzymes

PDB ID 1lq7

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