6AAE

Crystal structure of Chloramphenicol-Metabolizaing Enzyme EstDL136

Summary for 6AAE

• Entry DOI: 10.2210/pdb6aae/pdb
• Descriptor: Esterase, PENTAETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: chloramphenicol, metagenome, hornome sensitive lipase, hsl, estdl136, esterase, hydrolase
• Biological source: uncultured bacterium
• Total number of polymer chains: 2
• Total formula weight: 71267.82

Authors

Kim, S.H.,Kang, P.A.,Han, K.T.,Lee, S.W.,Rhee, S.K. (deposition date: 2018-07-18, release date: 2019-02-06, Last modification date: 2023-11-22)

Primary citation

Kim, S.H.,Kang, P.A.,Han, K.T.,Lee, S.W.,Rhee, S.K.
Crystal structure of chloramphenicol-metabolizing enzyme EstDL136 from a metagenome.
PLoS ONE, 14:e0210298-e0210298, 2019

PubMed Abstract: Metagenomes often convey novel biological activities and therefore have gained considerable attention for use in biotechnological applications. Recently, metagenome-derived EstDL136 was found to possess chloramphenicol (Cm)-metabolizing features. Sequence analysis showed EstDL136 to be a member of the hormone-sensitive lipase (HSL) family with an Asp-His-Ser catalytic triad and a notable substrate specificity. In this study, we determined the crystal structures of EstDL136 and in a complex with Cm. Consistent with the high sequence similarity, the structure of EstDL136 is homologous to that of the HSL family. The active site of EstDL136 is a relatively shallow pocket that could accommodate Cm as a substrate as opposed to the long acyl chain substrates typical of the HSL family. Mutational analyses further suggested that several residues in the vicinity of the active site play roles in the Cm-binding of EstDL136. These results provide structural and functional insights into a metagenome-derived EstDL136.

PubMed: 30645605
DOI: 10.1371/journal.pone.0210298

Experimental method

X-RAY DIFFRACTION (1.641 Å)