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.


2cak

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cak.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2cak.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cak| PDB=2cak | SCENE= }}
{{STRUCTURE_2cak| PDB=2cak | SCENE= }}
-
'''1.27ANGSTROM STRUCTURE OF RUSTICYANIN FROM THIOBACILLUS FERROOXIDANS'''
+
===1.27ANGSTROM STRUCTURE OF RUSTICYANIN FROM THIOBACILLUS FERROOXIDANS===
-
==Overview==
+
<!--
-
Rusticyanin from the extremophile Thiobacillus ferrooxidans is a blue copper protein with unusually high redox potential and acid stability. We present the crystal structures of native rusticyanin and of its Cu site mutant His143Met at 1.27 and 1.10 A, respectively. The very high resolution of these structures allows a direct comparison with EXAFS data and with quantum chemical models of the oxidized and reduced forms of the proteins, based upon both isolated and embedded clusters and density functional theory (DFT) methods. We further predict the structure of the Cu(II) form of the His143Met mutant which has been experimentally inaccessible due to its very high redox potential. We also present metrical EXAFS data and quantum chemical calculations for the oxidized and reduced states of the Met148Gln mutant, this protein having the lowest redox potential of all currently characterized mutants of rusticyanin. These data offer new insights into the structural factors which affect the redox potential in this important class of proteins. Calculations successfully predict the structure and the order of redox potentials for the three proteins. The calculated redox potential of H143M ( approximately 400 mV greater than native rusticyanin) is consistent with the failure of readily available chemical oxidants to restore a Cu(II) species of this mutant. The structural and energetic effects of mutating the equatorial cysteine to serine, yet to be studied experimentally, are predicted to be considerable by our calculations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16503647}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16503647 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16503647}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Rusticyanin]]
[[Category: Rusticyanin]]
[[Category: Transport]]
[[Category: Transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:35:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:34:05 2008''

Revision as of 16:34, 27 July 2008

Image:2cak.png

Template:STRUCTURE 2cak

1.27ANGSTROM STRUCTURE OF RUSTICYANIN FROM THIOBACILLUS FERROOXIDANS

Template:ABSTRACT PUBMED 16503647

About this Structure

2CAK is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties., Barrett ML, Harvey I, Sundararajan M, Surendran R, Hall JF, Ellis MJ, Hough MA, Strange RW, Hillier IH, Hasnain SS, Biochemistry. 2006 Mar 7;45(9):2927-39. PMID:16503647

Page seeded by OCA on Sun Jul 27 19:34:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cak"
Personal tools