This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1aen
From Proteopedia
(New page: 200px<br /> <applet load="1aen" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aen, resolution 2.1Å" /> '''SPECIFICITY OF LIGAN...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1AEN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 25T as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEN OCA]]. | + | 1AEN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 25T as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEN OCA]]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:38:06 2007'' |
Revision as of 06:33, 30 October 2007
|
SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (2-AMINO-5-METHYLTHIAZOLE)
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
1AEN is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and 25T as [ligands]. Active as [Oxidoreductase], with EC number [1.11.1.5]. Structure known Active Site: AVE. 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
Page seeded by OCA on Tue Oct 30 08:38:06 2007
