1d3w: Difference between revisions
New page: left|200px<br /><applet load="1d3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d3w, resolution 1.7Å" /> '''Crystal structure of ... |
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[[Image:1d3w.gif|left|200px]]<br /><applet load="1d3w" size=" | [[Image:1d3w.gif|left|200px]]<br /><applet load="1d3w" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1d3w, resolution 1.7Å" /> | caption="1d3w, resolution 1.7Å" /> | ||
'''Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.'''<br /> | '''Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.'''<br /> | ||
==Overview== | ==Overview== | ||
The basis of the chemiosmotic theory is that energy from light or | 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 Structure== | ==About this Structure== | ||
1D3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with SF4 and F3S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1D3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3W OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Armstrong, F | [[Category: Armstrong, F A.]] | ||
[[Category: Bonagura, C | [[Category: Bonagura, C A.]] | ||
[[Category: Burges, B | [[Category: Burges, B K.]] | ||
[[Category: Camba, R.]] | [[Category: Camba, R.]] | ||
[[Category: Chen, K.]] | [[Category: Chen, K.]] | ||
[[Category: Hirst, J.]] | [[Category: Hirst, J.]] | ||
[[Category: Stout, C | [[Category: Stout, C D.]] | ||
[[Category: F3S]] | [[Category: F3S]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
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[[Category: protein monomer]] | [[Category: protein monomer]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:44 2008'' | ||
Revision as of 13:12, 21 February 2008
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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 with and as ligands. 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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