1W9M

AS-isolated hybrid cluster protein from Desulfovibrio vulgaris X-ray structure at 1.35A resolution using iron anomalous signal

1W9M の概要

• エントリーDOI: 10.2210/pdb1w9m/pdb
• 関連するPDBエントリー: 1E1D 1E2U 1E9V 1GNT 1OA1
• 分子名称: HYDROXYLAMINE REDUCTASE, IRON/SULFUR CLUSTER, FE-S-O HYBRID CLUSTER, ... (4 entities in total)
• 機能のキーワード: hybrid cluster protein, anaerobic, oxidised, as-isolated, desulfovibrio vulgaris, oxidoreductase
• 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: 60761.85

構造登録者

Aragao, D.,Macedo, S.,Mitchell, E.P.,Coelho, D.,Romao, C.V.,Teixeira, M.,Lindley, P.F. (登録日: 2004-10-14, 公開日: 2005-02-04, 最終更新日: 2024-10-16)

主引用文献

Aragao, D.,Mitchell, E.P.,Frazao, C.F.,Carrondo, M.A.,Lindley, P.F.
Structural and Functional Relationships in the Hybrid Cluster Protein Family:Structure of the Anaerobically Purified Hybrid Cluster Protein from Desulfovibrio Vulgaris at 1.35 A Resolution
Acta Crystallogr.,Sect.D, 64:665-, 2008

PubMed Abstract: The hybrid cluster protein (HCP) from the sulfate-reducing bacterium Desulfovibrio vulgaris strain Hildenborough has been isolated and crystallized anaerobically. The phase problem was solved for a P2(1)2(1)2(1) crystal form using multiple-wavelength anomalous diffraction data collected in the vicinity of the Fe K absorption edge. Although the overall protein structure is essentially the same as that previously obtained, it shows that the nature of the hybrid cluster has particular differences when isolated and crystallized in the absence of oxygen and this provides insight into the structural features associated with changes in the oxidation state. A comparison between HCPs and carbon monoxide dehydrogenases (CoDs) shows that they possess a similar fold and that the dehydrogenases have a related cluster at the equivalent HCP hybrid cluster position. This helps to understand the nature of the hybrid cluster and to predict a dimeric structure for class 3 HCPs, which lack the N-terminal region.

PubMed: 18560155
DOI: 10.1107/S0907444908009165

実験手法

X-RAY DIFFRACTION (1.35 Å)