Wherland Sandbox 2

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Revision as of 06:37, 9 July 2015

This is a default text for your page Wherland Sandbox 2. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Intramolecular Electron Transfer in Azurin
2 Function
3 Disease
4 Relevance
5 Structural highlights
6 References

Intramolecular Electron Transfer in Azurin

Introduction

Azurin is a bacterial protein that has been extensively studied by bioinorganic and biophysical chemists as a prototype of a Type 1 or "blue" copper protein. It contains a single copper ion that can be in the Cu⁺ or Cu²⁺ or the Cu state. The intensely blue color is due to a charge transfer transition from the cysteine thiolate ligand to the Cu in the Cu²⁺ state. It functions as an electron transfer mediator. The electron transfer reactivity of azurin has been extensively studied, including studies of its reactivity with natural and artificial partners, and intramolecular electron transfer from intrinsic and covalently attached electron transfer partners. The latter studies have been instrumental in defining and evaluating the factors influencing electron transfer reactivity through proteins. These factors include the electron transfer distance, the structure of the intervening peptide medium, the thermodynamic driving force, and the structure of the donor and acceptor. These studies have been instrumental in the iterative testing and advancing of electron transfer theory. One series of studies, delineated here, involves measurement of the rate constant for electron transfer from a disulfide radical, produced by pulse radiolysis, to the Cu²⁺ ion. This reaction can be made to occur because of particular structural features of azurin, the Cu²⁺ site is relatively buried and at the opposite end of the protein from the only disulfide, which is exposed to solvent and electron transfer reagents.

Structure

Azurin has 128 amino acids and a beta barrel structure, as exemplified by the structure of the Pseudomonas aeruginosa protein (4AZUA, chain A). The is shown colored by the secondary structure assignment (pink for alpha helix, purple for a 310 helix, yellow for beta strands, blue for beta turns, and white for other structures). The copper atom is at the top of this standard orientation. The primary ligands to the copper atom are the thiolate of Cys112, and ND His117 and His 46, forming a trigonal planar arrangement. In addition there are two weaker ligands, the S of Met121 and the carbonyl O of Gly45, occupying axial positions to give an approximately trigonal bipyramidal

Function

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Scot Wherland

Retrieved from "http://52.214.119.220/wiki/index.php/Wherland_Sandbox_2"

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 This is a default text for your page '''Wherland Sandbox 2'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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 == Structure ==
 Azurin has 128 amino acids and a beta barrel structure, as exemplified by the structure of the ''Pseudomonas aeruginosa'' protein (4AZUA, chain A).  The
-<scene name='70/703985/Azurin_a_backbone/1'>TextToBeDisplayed</scene> is shown colored by the secondary structure assignment (pink for alpha helix, purple for a 310 helix, yellow for beta strands, blue for beta turns, and white for other structures).  The copper atom is at the top of this standard orientation.  The primary ligands to the copper atom are the thiolate of Cys112, and ND His117 and His 46, forming a trigonal planar arrangement.  In addition there are two weaker ligands, the S of Met121 and the carbonyl O of Gly45, occupying axial positions to give an approximately trigonal bipyramidal
+<scene name='70/703985/Azurin_a_backbone/1'>Backbone</scene> is shown colored by the secondary structure assignment (pink for alpha helix, purple for a 310 helix, yellow for beta strands, blue for beta turns, and white for other structures).  The copper atom is at the top of this standard orientation.  The primary ligands to the copper atom are the thiolate of Cys112, and ND His117 and His 46, forming a trigonal planar arrangement.  In addition there are two weaker ligands, the S of Met121 and the carbonyl O of Gly45, occupying axial positions to give an approximately trigonal bipyramidal
 </StructureSection>
 == Function ==

Wherland Sandbox 2

From Proteopedia

Revision as of 06:37, 9 July 2015

Contents

Intramolecular Electron Transfer in Azurin

Introduction

Structure

Function

Disease

Relevance

Structural highlights

References

Proteopedia Page Contributors and Editors (what is this?)

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