1d3w: Difference between revisions
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|PDB= 1d3w |SIZE=350|CAPTION= <scene name='initialview01'>1d3w</scene>, resolution 1.7Å | |PDB= 1d3w |SIZE=350|CAPTION= <scene name='initialview01'>1d3w</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1fdd|1FDD]], [[1bot|1BOT]], [[6fdr|6FDR]], [[7fdr|7FDR]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3w OCA], [http://www.ebi.ac.uk/pdbsum/1d3w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d3w RCSB]</span> | |||
}} | }} | ||
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[[Category: Hirst, J.]] | [[Category: Hirst, J.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| Line 37: | Line 38: | ||
[[Category: protein monomer]] | [[Category: protein monomer]] | ||
''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 19:34:07 2008'' | ||
Revision as of 19:34, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1FDD, 1BOT, 6FDR, 7FDR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.
OverviewOverview
The basis of the chemiosmotic theory is that energy from light or respiration is used to generate a trans-membrane proton gradient. This is largely achieved by membrane-spanning enzymes known as 'proton pumps. There is intense interest in experiments which reveal, at the molecular level, how protons are drawn through proteins. Here we report the mechanism, at atomic resolution, for a single long-range electron-coupled proton transfer. In Azotobacter vinelandii ferredoxin I, reduction of a buried iron-sulphur cluster draws in a solvent proton, whereas re-oxidation is 'gated' by proton release to the solvent. Studies of this 'proton-transferring module' by fast-scan protein film voltammetry, high-resolution crystallography, site-directed mutagenesis and molecular dynamics, reveal that proton transfer is exquisitely sensitive to the position and pK of a single amino acid. The proton is delivered through the protein matrix by rapid penetrative excursions of the side-chain carboxylate of a surface residue (Asp 15), whose pK shifts in response to the electrostatic charge on the iron-sulphur cluster. Our analysis defines the structural, dynamic and energetic requirements for proton courier groups in redox-driven proton-pumping enzymes.
About this StructureAbout this Structure
1D3W is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
ReferenceReference
Atomically defined mechanism for proton transfer to a buried redox centre in a protein., Chen K, Hirst J, Camba R, Bonagura CA, Stout CD, Burgess BK, Armstrong FA, Nature. 2000 Jun 15;405(6788):814-7. PMID:10866206
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