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1h1o

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[[Image:1h1o.gif|left|200px]]<br />
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[[Image:1h1o.gif|left|200px]]<br /><applet load="1h1o" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1h1o" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1h1o, resolution 2.13&Aring;" />
caption="1h1o, resolution 2.13&Aring;" />
'''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER'''<br />
'''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER'''<br />
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==About this Structure==
==About this Structure==
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1H1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans] with SO4, ZN, HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: GOL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1O OCA].
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1H1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans] with SO4, ZN, HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=GOL:Zn Binding Site For Chain B'>GOL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1O OCA].
==Reference==
==Reference==
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[[Category: heme]]
[[Category: heme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:25:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:52:30 2007''

Revision as of 13:42, 18 December 2007

Image:1h1o.gif

1h1o, resolution 2.13Å

Drag the structure with the mouse to rotate

ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER

Overview

The study of electron transfer between the copper protein rusticyanin, (RCy) and the c(4)-cytochrome CYC(41) of the acidophilic bacterium, Acidithiobacillus ferrooxidans has evidenced a remarkable decrease of, RCy's redox potential upon complex formation. The structure of the CYC(41), obtained at 2.2 A resolution highlighted a specific glutamate residue, (E121) involved in zinc binding as potentially playing a central role in, this effect, required for the electron transfer to occur. EPR and, stopped-flow experiments confirmed the strong inhibitory effect of, divalent cations on CYC(41):RCy complex formation. A docking analysis of, the CYC(41) and RCy structure allows us to propose a detailed model for, the complex-induced tuning of electron transfer in agreement with our, experimental data, which could be representative of other copper proteins, involved in electron transfer.

About this Structure

1H1O is a Single protein structure of sequence from Acidithiobacillus ferrooxidans with SO4, ZN, HEM and GOL as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The structure of Acidithiobacillus ferrooxidans c(4)-cytochrome: a model for complex-induced electron transfer tuning., Abergel C, Nitschke W, Malarte G, Bruschi M, Claverie JM, Giudici-Orticoni MT, Structure. 2003 May;11(5):547-55. PMID:12737820

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