1n9c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1n9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n9c" /> '''Structure and dynamics of reduced Bacillus p...)
Line 1: Line 1:
-
[[Image:1n9c.jpg|left|200px]]<br /><applet load="1n9c" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1n9c.jpg|left|200px]]<br /><applet load="1n9c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n9c" />
caption="1n9c" />
'''Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes'''<br />
'''Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes'''<br />
==Overview==
==Overview==
-
The solution structure of reduced Bacillus pasteurii cytochrome c, which, has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/-, 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and, refined through restrained energy minimization. The target function out of, 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/-, 12 kJ mol(-)(1). The structure appears very similar to that in the, oxidized state, only Trp87 and the propionates showing significant, differences. The mobility was investigated through (15)N R(1) and R(2), relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that, the oxidized form is generally more mobile than the reduced one. By, comparing the redox-state dependence of the structural/dynamic properties, of Fe-S proteins, cytochrome c, and blue copper proteins, hints are, provided for a better comprehension of the electron transfer processes.
+
The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.
==About this Structure==
==About this Structure==
-
1N9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N9C OCA].
+
1N9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9C OCA].
==Reference==
==Reference==
Line 22: Line 22:
[[Category: respiration]]
[[Category: respiration]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:04:25 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:38 2008''

Revision as of 12:03, 21 February 2008


1n9c

Drag the structure with the mouse to rotate

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes

Overview

The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.

About this Structure

1N9C is a Single protein structure of sequence from Sporosarcina pasteurii with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes., Bartalesi I, Bertini I, Rosato A, Biochemistry. 2003 Jan 28;42(3):739-45. PMID:12534286

Page seeded by OCA on Thu Feb 21 14:03:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools