1h1o

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[[Image:1h1o.gif|left|200px]]
[[Image:1h1o.gif|left|200px]]
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{{Structure
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|PDB= 1h1o |SIZE=350|CAPTION= <scene name='initialview01'>1h1o</scene>, resolution 2.13&Aring;
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The line below this paragraph, containing "STRUCTURE_1h1o", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=GOL:Zn+Binding+Site+For+Chain+B'>GOL</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1h1o| PDB=1h1o | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1o OCA], [http://www.ebi.ac.uk/pdbsum/1h1o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h1o RCSB]</span>
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'''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER'''
'''ACIDITHIOBACILLUS FERROOXIDANS CYTOCHROME C4 STRUCTURE SUPPORTS A COMPLEX-INDUCED TUNING OF ELECTRON TRANSFER'''
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[[Category: Malarte, G.]]
[[Category: Malarte, G.]]
[[Category: Nitschke, W.]]
[[Category: Nitschke, W.]]
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[[Category: c4]]
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[[Category: C4]]
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[[Category: cytochrome]]
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[[Category: Cytochrome]]
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[[Category: electron transfer]]
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[[Category: Electron transfer]]
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[[Category: heme]]
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[[Category: Heme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:18:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:51 2008''
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Revision as of 15:18, 2 May 2008

Image:1h1o.gif

Template:STRUCTURE 1h1o

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 Fri May 2 18:18:27 2008

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