1aeq
From Proteopedia
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(New page: 200px<br /> <applet load="1aeq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aeq, resolution 2.1Å" /> '''VARIATION IN THE STR...)
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Revision as of 14:23, 29 October 2007
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VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2-ETHYLIMIDAZOLE)
Overview
Cavity complementation has been observed in many proteins, where an, appropriate small molecule binds to a cavity-forming mutant. Here, the, binding of compounds to the W191G cavity mutant of cytochrome c peroxidase, is characterized by X-ray crystallography and binding thermodynamics., Unlike cavities created by removal of hydrophobic side-chains, the W191G, cavity does not bind neutral or hydrophobic compounds, but displays a, strong specificity for heterocyclic cations, consistent with the role of, the protein to stabilize a tryptophan radical at this site. Ligand, dissociation constants for the protonated cationic state ranged from 6, microM for 2-amino-5-methylthiazole to 1 mM for neutral ligands, and, binding was associated with a large enthalpy-entropy compensation. X-ray, ... [(full description)]
About this Structure
1AEQ is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and 2EZ as [ligands]. Active as [[1]], with EC number [1.11.1.5]. Full crystallographic information is available from [OCA].
Reference
Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein., Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, J Mol Biol. 2002 Jan 25;315(4):845-57. PMID:11812152
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