1lq7
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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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[[Category: three helix bundle]] | [[Category: three helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:57 2008'' |
Revision as of 19:06, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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