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| Hauptseite > Publikationsdatenbank > Pseudomonas aeruginosa esterase PA2949, a bacterial homolog of the human membrane esterase ABHD6: expression, purification and crystallization > print |
| Hauptseite > Publikationsdatenbank > Pseudomonas aeruginosa esterase PA2949, a bacterial homolog of the human membrane esterase ABHD6: expression, purification and crystallization > print |
| 001 | 862156 | ||
| 005 | 20210130001207.0 | ||
| 024 | 7 | _ | |a 10.1107/S2053230X19002152 |2 doi |
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| 245 | _ | _ | |a Pseudomonas aeruginosa esterase PA2949, a bacterial homolog of the human membrane esterase ABHD6: expression, purification and crystallization |
| 260 | _ | _ | |a Oxford [u.a.] |c 2019 |b Blackwell |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a The human membrane-bound α/β-hydrolase domain 6 (ABHD6) protein modulates endocannabinoid signaling, which controls appetite, pain and learning, as well as being linked to Alzheimer's and Parkinson's diseases, through the degradation of the key lipid messenger 2-arachidonylglycerol (2-AG). This makes ABHD6 an attractive therapeutic target that lacks structural information. In order to better understand the molecular mechanism of 2-AG-hydrolyzing enzymes, the PA2949 protein from Pseudomonas aeruginosa, which has 49% sequence similarity to the ABHD6 protein, was cloned, overexpressed, purified and crystallized. Overexpression of PA2949 in the homologous host yielded the membrane-bound enzyme, which was purified in milligram amounts. Besides their sequence similarity, the enzymes both show specificity for the hydrolysis of 2-AG and esters of medium-length fatty acids. PA2949 in the presence of n-octyl β-D-glucoside showed a higher activity and stability at room temperature than those previously reported for PA2949 overexpressed and purified from Escherichia coli. A suitable expression host and stabilizing detergent were crucial for obtaining crystals, which belonged to the tetragonal space group I4122 and diffracted to a resolution of 2.54 Å. This study provides hints on the functional similarity of ABHD6-like proteins in prokaryotes and eukaryotes, and might guide the structural study of these difficult-to-crystallize proteins. |
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| 700 | 1 | _ | |a Batra-Safferling, Renu |0 P:(DE-Juel1)131950 |b 3 |e Corresponding author |u fzj |
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| 700 | 1 | _ | |a Kovacic, Filip |0 P:(DE-Juel1)131480 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.1107/S2053230X19002152 |g Vol. 75, no. 4, p. 270 - 277 |0 PERI:(DE-600)2175956-X |n 4 |p 270 - 277 |t Acta crystallographica / F Structural biology communications Section F |v F75 |y 2019 |x 2053-230X |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/862156/files/Bleffert-et-al-2019-revised-end_noColor.pdf |y OpenAccess |
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