1E2U

Low Temperature Structure of Hybrid Cluster Protein from Desulfovibrio vulgaris to 1.6A

1E2U の概要

• エントリーDOI: 10.2210/pdb1e2u/pdb
• 関連するPDBエントリー: 1E1D
• 分子名称: HYDROXYLAMINE REDUCTASE, IRON/SULFUR CLUSTER, IRON/SULFUR/OXYGEN HYBRID CLUSTER, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, cubane, iron sulfur, fuscoredoxin
• 由来する生物種: DESULFOVIBRIO VULGARIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60793.92

構造登録者

Cooper, S.J.,Bailey, S.,Hagen, W.R.,Lindley, P.F. (登録日: 2000-05-26, 公開日: 2000-12-11, 最終更新日: 2024-11-13)

主引用文献

Cooper, S.J.,Garner, C.D.,Hagen, W.R.,Lindley, P.F.,Bailey, S.
Hybrid-Cluster Protein (Hcp) from Desulfovibrio Vulgaris (Hildenborough) at 1.6 A Resolution.
Biochemistry, 39:15044-, 2000

PubMed Abstract: The three-dimensional structure of the hybrid cluster protein from Desulfovibrio vulgaris (Hildenborough) has been determined at 1.6 A resolution using synchrotron X-ray radiation. The protein can be divided into three domains: an N-terminal mainly alpha-helical domain and two similar domains comprising a central beta-sheet flanked by alpha-helices. The protein contains two 4Fe clusters with an edge-to-edge distance of 10.9 A. Four cysteine residues at the N-terminus of the protein are ligands to the iron atoms of a conventional [4Fe-4S] cubane cluster. The second cluster has an unusual asymmetric structure and has been named the hybrid cluster to reflect the variety of protein ligands, namely two mu-sulfido bridges, two mu(2)-oxo bridges, and a further disordered bridging ligand. Anomalous differences in data collected at 1.488 A and close to the iron edge at 1.743 A have been used to confirm the identity of the metal and sulfur atoms. The hybrid cluster is buried in the center of the protein, but is accessible through a large hydrophobic cavity that runs the length of domain 3. Hydrophobic channels have previously been identified as access routes to the active centers in redox enzymes with gaseous substrates. The hybrid cluster is also accessible by a hydrophilic channel. The [4Fe-4S] cubane cluster is close to an indentation on the surface of the protein and can also be approached on the opposite side by a long solvent channel. At the present time, neither the significance of these channels nor, indeed, the function of the hybrid cluster protein is known.

PubMed: 11106482
DOI: 10.1021/BI001483M

実験手法

X-RAY DIFFRACTION (1.6 Å)