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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of an aryl esterase from Pseudomonas fluorescens.
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Structure of an aryl esterase from Pseudomonas fluorescens.

机译：假单胞菌的芳基酯酶的结构的荧光。

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摘要

The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 A by X-ray diffraction and shows a characteristic alpha/beta-hydrolase fold. In addition to catalyzing the hydrolysis of esters in vitro, PFE also shows low bromoperoxidase activity. PFE shows highest structural similarity, including the active-site environment, to a family of non-heme bacterial haloperoxidases, with an r.m.s. deviation in 271 C(alpha) atoms between PFE and its five closest structural neighbors averaging 0.8 A. PFE has far less similarity (r.m.s. deviation in 218 C(alpha) atoms of 5.0 A) to P. fluorescens carboxyl esterase. PFE favors activated esters with small acyl groups, such as phenyl acetate. The X-ray structure of PFE reveals a significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups.
机译：工业结构的芳基酯酶荧光假单胞菌,已经解决了通过x射线衍射和1.8的分辨率显示了特有的α/ beta-hydrolase褶皱。除了催化的水解酯体外,pfizer还显示低bromoperoxidase活动。结构相似,包括活性部位环境,家庭非血红素的细菌271年haloperoxidases, r.m.s.偏差C(α)原子之间的工业和它的五个最亲密的结构性邻居场均0.8。少相似(r.m.s.偏差在218 C(α)5.0) p原子荧光羧基酯酶。酰基团体,如苯乙酸。工业结构揭示了一个明显的阻挡活跃的站点。包括Trp28和Met95,限制的大小acyl-binding口袋,解释其偏好对于小型酰基组。

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