2vkr
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="2vkr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vkr, resolution 2.01Å" /> '''3FE-4S, 4FE-4S PLUS ...)
Next diff →
Revision as of 11:23, 5 March 2008
|
3FE-4S, 4FE-4S PLUS ZN ACIDIANUS AMBIVALENS FERREDOXIN
Overview
Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0A resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn(2+) site and the ferredoxin (betaalphabeta)(2) core, which harbours intact clusters I and II, a [3Fe-4S](1+/0) and a [4Fe-4S](2+/1+) centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S](1+/0) centres and poor definition around cluster II.
About this Structure
2VKR is a Single protein structure of sequence from Acidianus ambivalens with , and as ligands. Known structural/functional Sites: , , , , , , , , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+)-containing ferredoxin., Frazao C, Aragao D, Coelho R, Leal SS, Gomes CM, Teixeira M, Carrondo MA, FEBS Lett. 2008 Mar 5;582(5):763-7. Epub 2008 Feb 5. PMID:18258200
Page seeded by OCA on Wed Mar 5 13:23:02 2008
Categories: Acidianus ambivalens | Single protein | Aragao, D. | Carrondo, M A. | Coelho, R. | Frazao, C. | Gomes, C M. | Leal, S S. | Teixeira, M. | F3S | SF4 | ZN | 3fe-4 | 4fe-4 | Electron transport | Ferredoxin | Hemihedric twinnig | Iron | Iron-sulfur | Iron-sulfur protein | Metal-binding | Methylation | Protein folding | Thermophile | Thermostable protein | Transport | Zinc | Zn center