This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1d3w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1d3w.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1d3w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1d3w| PDB=1d3w | SCENE= }}
{{STRUCTURE_1d3w| PDB=1d3w | SCENE= }}
-
'''Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.'''
+
===Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10866206}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10866206 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10866206}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Iron-sulphur protein]]
[[Category: Iron-sulphur protein]]
[[Category: Protein monomer]]
[[Category: Protein monomer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:25:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:21:01 2008''

Revision as of 19:21, 30 June 2008

Image:1d3w.png

Template:STRUCTURE 1d3w

Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.

Template:ABSTRACT PUBMED 10866206

About this Structure

1D3W is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jun 30 22:21:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d3w"
Personal tools