1h1o
From Proteopedia
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|PDB= 1h1o |SIZE=350|CAPTION= <scene name='initialview01'>1h1o</scene>, resolution 2.13Å | |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> | |SITE= <scene name='pdbsite=GOL:Zn+Binding+Site+For+Chain+B'>GOL</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Malarte, G.]] | [[Category: Malarte, G.]] | ||
[[Category: Nitschke, W.]] | [[Category: Nitschke, W.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: c4]] | [[Category: c4]] | ||
[[Category: cytochrome]] | [[Category: cytochrome]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:51 2008'' |
Revision as of 17:55, 30 March 2008
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| , resolution 2.13Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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