Evidence map›Paper›PMID 39718026›Full record

ArticleActa crystallographica. Section F, Structural biology communications2025

Crystallization and preliminary X-ray crystallographic studies of AfeH from Acimetobacter sp. DL-2.

Huiling Tang, XiaoRan Zhang, Yajuan Duan, Yan Huang

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Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Huiling TangDepartment of Scientific Research Office, Jiangsu Food and Pharmaceutical Science College, Huai'an 223003, People's Republic of China.
XiaoRan ZhangKey Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture and Rural Affairs, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.
Yajuan DuanKey Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture and Rural Affairs, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.
Yan HuangKey Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture and Rural Affairs, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fenoxaprop-P-ethyl (FE) is widely applied as a post-emergence aryloxyphenoxy propionate (AOPP) herbicide in agriculture. A novel FE hydrolase esterase from Acinetobacter sp. DL-2 (AfeH) was identified which belongs to the family IV carboxylesterases and shows less than 30% identity to other reported homologues with known structure. In order to understand the catalytic mechanism, recombinant AfeH was prepared in Escherichia coli and crystallized using the sitting-drop vapor-diffusion method. X-ray diffraction data were collected to 1.9 Å resolution. The crystal belonged to space group P12

Indexed as

CrystallizationAcinetobacterAmino Acid SequenceBacterial ProteinsCloning, MolecularCrystallography, X-RayEscherichia coliRecombinant ProteinsBacterial ProteinsRecombinant ProteinsAcimetobacter sp. DL-2AfeHcarboxylesterasesfamily IVX-ray crystallography

Identifiers

PMID39718026
PMCPMC11701925

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