1h1o
From Proteopedia
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| - | [[Image:1h1o.gif|left|200px]]<br /><applet load="1h1o" size=" | + | [[Image:1h1o.gif|left|200px]]<br /><applet load="1h1o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h1o, resolution 2.13Å" /> | caption="1h1o, resolution 2.13Å" /> | ||
'''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== | ||
| - | 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:// | + | 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 <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:11 2008'' |
Revision as of 07:45, 3 February 2008
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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 , , and 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
Page seeded by OCA on Sun Feb 3 09:45:11 2008
Categories: Acidithiobacillus ferrooxidans | Single protein | Abergel, C. | Bruschi, M. | Claverie, J.M. | Guidici-Orticoni, M.T. | Malarte, G. | Nitschke, W. | GOL | HEM | SO4 | ZN | C4 | Cytochrome | Electron transfer | Heme
