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@ARTICLE{Rengachari:141360,
      author       = {Rengachari, S. and Bezerra, G. A. and Riegler-Berket, L.
                      and Gruber, C. C. and Sturm, C. and Taschler, U. and
                      Boeszoermenyi, A. and Dreveny, I. and Zimmermann, R. and
                      Gruber, K. and Oberer, M. and DESY},
      title        = {{T}he structure of monoacylglycerol lipase from {B}acillus
                      sp. {H}257 reveals unexpected conservation of the cap
                      architecture between bacterial and human enzymes},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1821},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-25482},
      pages        = {1012-1021},
      year         = {2012},
      note         = {(c) Elsevier B.V. Code P.},
      abstract     = {Monoacylglycerol lipases (MGLs) catalyse the hydrolysis of
                      monoacylglycerol into free fatty acid and glycerol. MGLs
                      have been identified throughout all genera of life and have
                      adopted different substrate specificities depending on their
                      physiological role. In humans, MGL plays an integral part in
                      lipid metabolism affecting energy homeostasis, signalling
                      processes and cancer cell progression. In bacteria, MGLs
                      degrade short-chain monoacylglycerols which are otherwise
                      toxic to the organism. We report the crystal structures of
                      MGL from the bacterium Bacillus sp. H257 (bMGL) in its free
                      form at 1.2Å and in complex with phenylmethylsulfonyl
                      fluoride at 1.8Å resolution. In both structures, bMGL
                      adopts an α/β hydrolase fold with a cap in an open
                      conformation. Access to the active site residues, which were
                      unambiguously identified from the protein structure, is
                      facilitated by two different channels. The larger channel
                      constitutes the highly hydrophobic substrate binding pocket
                      with enough room to accommodate monoacylglycerol. The other
                      channel is rather small and resembles the proposed glycerol
                      exit hole in human MGL. Molecular dynamics simulation of
                      bMGL yielded open and closed states of the entrance channel
                      and the glycerol exit hole. Despite differences in the
                      number of residues, secondary structure elements, and low
                      sequence identity in the cap region, this first structure of
                      a bacterial MGL reveals striking structural conservation of
                      the overall cap architecture in comparison with human MGL.
                      Thus it provides insight into the structural conservation of
                      the cap amongst MGLs throughout evolution and provides a
                      framework for rationalising substrate specificities in each
                      organism.},
      keywords     = {Amino Acid Sequence / Bacillus: enzymology / Bacillus:
                      genetics / Bacterial Proteins: chemistry / Bacterial
                      Proteins: genetics / Bacterial Proteins: metabolism /
                      Catalytic Domain / Cloning, Molecular / Conserved Sequence /
                      Crystallography, X-Ray / Escherichia coli / Humans /
                      Hydrophobic and Hydrophilic Interactions / Molecular
                      Dynamics Simulation / Molecular Sequence Data /
                      Monoacylglycerol Lipases: chemistry / Monoacylglycerol
                      Lipases: genetics / Monoacylglycerol Lipases: metabolism /
                      Monoglycerides: chemistry / Monoglycerides: metabolism /
                      Phenylmethylsulfonyl Fluoride: chemistry / Protein
                      Structure, Secondary / Recombinant Proteins: chemistry /
                      Recombinant Proteins: genetics / Recombinant Proteins:
                      metabolism / Sequence Alignment / Structural Homology,
                      Protein / Substrate Specificity / Bacterial Proteins (NLM
                      Chemicals) / Monoglycerides (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals) / Phenylmethylsulfonyl Fluoride
                      (NLM Chemicals) / Monoacylglycerol Lipases (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22561231},
      UT           = {WOS:000305359200009},
      doi          = {10.1016/j.bbalip.2012.04.006},
      url          = {https://bib-pubdb1.desy.de/record/141360},
}