1lq7

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[[Image:1lq7.jpg|left|200px]]
[[Image:1lq7.jpg|left|200px]]
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{{Structure
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|PDB= 1lq7 |SIZE=350|CAPTION= <scene name='initialview01'>1lq7</scene>
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The line below this paragraph, containing "STRUCTURE_1lq7", creates the "Structure Box" on the page.
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{{STRUCTURE_1lq7| PDB=1lq7 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lq7 OCA], [http://www.ebi.ac.uk/pdbsum/1lq7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lq7 RCSB]</span>
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'''De Novo Designed Protein Model of Radical Enzymes'''
'''De Novo Designed Protein Model of Radical Enzymes'''
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==About this Structure==
==About this Structure==
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1LQ7 is a [[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].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ7 OCA].
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/12224922 12224922]
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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[[Category: ]]
 
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[[Category: Protein complex]]
 
[[Category: Blomberg, M.]]
[[Category: Blomberg, M.]]
[[Category: Dai, Q H.]]
[[Category: Dai, Q H.]]
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[[Category: Tommos, C.]]
[[Category: Tommos, C.]]
[[Category: Wand, A J.]]
[[Category: Wand, A J.]]
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[[Category: three helix bundle]]
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[[Category: Three helix bundle]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:57 2008''
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Revision as of 21:10, 2 May 2008

Template:STRUCTURE 1lq7

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

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 Page seeded by OCA on Sat May 3 00:10:08 2008

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