1lq7
From Proteopedia
(New page: 200px<br /><applet load="1lq7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lq7" /> '''De Novo Designed Protein Model of Radical En...) |
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| - | [[Image:1lq7.jpg|left|200px]]<br /><applet load="1lq7" size=" | + | [[Image:1lq7.jpg|left|200px]]<br /><applet load="1lq7" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''De Novo Designed Protein Model of Radical Enzymes'''<br /> | '''De Novo Designed Protein Model of Radical Enzymes'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The use of side chains as catalytic cofactors for protein mediated redox | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1LQ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1LQ7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Blomberg, M.]] | [[Category: Blomberg, M.]] | ||
| - | [[Category: Dai, Q | + | [[Category: Dai, Q H.]] |
| - | [[Category: Dutton, P | + | [[Category: Dutton, P L.]] |
| - | [[Category: Fuentes, E | + | [[Category: Fuentes, E J.]] |
[[Category: Tommos, C.]] | [[Category: Tommos, C.]] | ||
| - | [[Category: Wand, A | + | [[Category: Wand, A J.]] |
[[Category: three helix bundle]] | [[Category: three helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:18 2008'' |
Revision as of 11:47, 21 February 2008
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De Novo Designed Protein Model of Radical Enzymes
Overview
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.
About this Structure
1LQ7 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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 [[Category: ]]
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