1h1o
From Proteopedia
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- | [[Image:1h1o.gif|left|200px]] | + | [[Image:1h1o.gif|left|200px]] |
- | + | ||
- | '''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER''' | + | {{Structure |
+ | |PDB= 1h1o |SIZE=350|CAPTION= <scene name='initialview01'>1h1o</scene>, resolution 2.13Å | ||
+ | |SITE= <scene name='pdbsite=GOL:Zn+Binding+Site+For+Chain+B'>GOL</scene> | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1H1O is a [ | + | 1H1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1O OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12737820 12737820] |
[[Category: Acidithiobacillus ferrooxidans]] | [[Category: Acidithiobacillus ferrooxidans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:01 2008'' |
Revision as of 09:31, 20 March 2008
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, resolution 2.13Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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. 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 Thu Mar 20 11:31:01 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