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@ARTICLE{Bleffert:862156,
      author       = {Bleffert, Florian and Granzin, Joachim and Gohlke, Holger
                      and Batra-Safferling, Renu and Jaeger, Karl-Erich and
                      Kovacic, Filip},
      title        = {{P}seudomonas aeruginosa esterase {PA}2949, a bacterial
                      homolog of the human membrane esterase {ABHD}6: expression,
                      purification and crystallization},
      journal      = {Acta crystallographica / F Structural biology
                      communications Section F},
      volume       = {F75},
      number       = {4},
      issn         = {2053-230X},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {FZJ-2019-02510},
      pages        = {270 - 277},
      year         = {2019},
      abstract     = {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.},
      cin          = {NIC / JSC / ICS-6 / IMET},
      ddc          = {530},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)IMET-20090612},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / 581 - Biotechnology (POF3-581) / 551 -
                      Functional Macromolecules and Complexes (POF3-551) /
                      Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / G:(DE-HGF)POF3-581 /
                      G:(DE-HGF)POF3-551 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30950828},
      UT           = {WOS:000463600400008},
      doi          = {10.1107/S2053230X19002152},
      url          = {https://juser.fz-juelich.de/record/862156},
}