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2CG2

Crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, in complex with sulfate

2CG2 の概要
エントリーDOI10.2210/pdb2cg2/pdb
関連するPDBエントリー2CFU 2CFZ 2CG3
分子名称SDSA1, SULFATE ION, ZINC ION, ... (4 entities in total)
機能のキーワードsds-hydrolase, sdsa1, pseudomonas aeruginosa, hydrolase
由来する生物種PSEUDOMONAS AERUGINOSA
タンパク質・核酸の鎖数1
化学式量合計72899.91
構造登録者
Hagelueken, G.,Adams, T.M.,Wiehlmann, L.,Widow, U.,Kolmar, H.,Tuemmler, B.,Heinz, D.W.,Schubert, W.-D. (登録日: 2006-02-27, 公開日: 2006-04-26, 最終更新日: 2023-12-13)
主引用文献Hagelueken, G.,Adams, T.M.,Wiehlmann, L.,Widow, U.,Kolmar, H.,Tummler, B.,Heinz, D.W.,Schubert, W.
The Crystal Structure of Sdsa1, an Alkylsulfatase from Pseudomonas Aeruginosa, Defines a Third Class of Sulfatases.
Proc.Natl.Acad.Sci.USA, 103:7631-, 2006
Cited by
PubMed Abstract: Pseudomonas aeruginosa is both a ubiquitous environmental bacterium and an opportunistic human pathogen. A remarkable metabolic versatility allows it to occupy a multitude of ecological niches, including wastewater treatment plants and such hostile environments as the human respiratory tract. P. aeruginosa is able to degrade and metabolize biocidic SDS, the detergent of most commercial personal hygiene products. We identify SdsA1 of P. aeruginosa as a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as SDS as a sole carbon or sulfur source. Homologues of SdsA1 are found in many pathogenic and some nonpathogenic bacteria. The crystal structure of SdsA1 reveals three distinct domains. The N-terminal catalytic domain with a binuclear Zn2+ cluster is a distinct member of the metallo-beta-lactamase fold family, the central dimerization domain ensures resistance to high concentrations of SDS, whereas the C-terminal domain provides a hydrophobic groove, presumably to recruit long aliphatic substrates. Crystal structures of apo-SdsA1 and complexes with substrate analog and products indicate an enzymatic mechanism involving a water molecule indirectly activated by the Zn2+ cluster. The enzyme SdsA1 thus represents a previously undescribed class of sulfatases that allows P. aeruginosa to survive and thrive under otherwise bacteriocidal conditions.
PubMed: 16684886
DOI: 10.1073/PNAS.0510501103
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 2cg2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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