1UWM

reduced ferredoxin 6 from Rhodobacter capsulatus

1UWM の概要

• エントリーDOI: 10.2210/pdb1uwm/pdb
• 関連するPDBエントリー: 1E9M
• 分子名称: FERREDOXIN VI, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: ferredoxin, electron transport, metal-binding, iron-sulfur, iron, 2fe-2s
• 由来する生物種: RHODOBACTER CAPSULATUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11590.85

構造登録者

Sainz, G.,Jakoncic, J.,Sieker, L.C.,Stojanoff, V.,Sanishvili, N.,Asso, M.,Bertrand, P.,Armengaud, J.,Jouanneau, Y. (登録日: 2004-02-05, 公開日: 2006-01-18, 最終更新日: 2023-12-13)

主引用文献

Sainz, G.,Jakoncic, J.,Sieker, L.C.,Stojanoff, V.,Sanishvili, N.,Asso, M.,Bertrand, P.,Armengaud, J.,Jouanneau, Y.
Structure of a [2Fe-2S] Ferredoxin from Rhodobacter Capsulatus Likely Involved in Fe-S Cluster Biogenesis and Conformational Changes Observed Upon Reduction.
J.Biol.Inorg.Chem., 11:235-, 2006

PubMed Abstract: FdVI from Rhodobacter capsulatus is structurally related to a group of [2Fe-2S] ferredoxins involved in iron-sulfur cluster biosynthesis. Comparative genomics suggested that FdVI and orthologs found in alpha-Proteobacteria are involved in this process. Here, the crystal structure of FdVI has been determined for both the oxidized and the reduced protein. The [2Fe-2S] cluster lies 6 A below the protein surface in a hydrophobic pocket without access to the solvent. This particular cluster environment might explain why the FdVI midpoint redox potential (-306 mV at pH 8.0) did not show temperature or ionic strength dependence. Besides the four cysteines that bind the cluster, FdVI features an extra cysteine which is located close to the S1 atom of the cluster and is oriented in a position such that its thiol group points towards the solvent. Upon reduction, the general fold of the polypeptide chain was almost unchanged. The [2Fe-2S] cluster underwent a conformational change from a planar to a distorted lozenge. In the vicinity of the cluster, the side chain of Met24 was rotated by 180 degrees , bringing its S atom within hydrogen-bonding distance of the S2 atom of the cluster. The reduced molecule also featured a higher content of bound water molecules, and more extensive hydrogen-bonding networks compared with the oxidized molecule. The unique conformational changes observed in FdVI upon reduction are discussed in the light of structural studies performed on related ferredoxins.

PubMed: 16402206
DOI: 10.1007/S00775-005-0069-2

実験手法

X-RAY DIFFRACTION (2 Å)