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@ARTICLE{PerezGarcia:890392,
      author       = {Perez-Garcia, Pablo and Kobus, Stefanie and Gertzen,
                      Christoph G. W. and Hoeppner, Astrid and Holzscheck,
                      Nicholas and Strunk, Christoph Heinrich and Huber, Harald
                      and Jaeger, Karl-Erich and Gohlke, Holger and Kovacic, Filip
                      and Smits, Sander H. J. and Streit, Wolfgang R. and Chow,
                      Jennifer},
      title        = {{A} promiscuous ancestral enzyme´s structure unveils
                      protein variable regions of the highly diverse
                      metallo-β-lactamase family},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-00925},
      pages        = {132},
      year         = {2021},
      abstract     = {The metallo-β-lactamase fold is an ancient protein
                      structure present in numerous enzyme families responsible
                      for diverse biological processes. The crystal structure of
                      the hyperthermostable crenarchaeal enzyme Igni18 from
                      Ignicoccus hospitalis was solved at 2.3 Å and could
                      resemble a possible first archetype of a multifunctional
                      metallo-β-lactamase. Ancestral enzymes at the evolutionary
                      origin are believed to be promiscuous all-rounders.
                      Consistently, Igni18´s activity can be cofactor-dependently
                      directed from β-lactamase to lactonase, lipase,
                      phosphodiesterase, phosphotriesterase or phospholipase. Its
                      core-domain is highly conserved within metallo-β-lactamases
                      from Bacteria, Archaea and Eukarya and gives insights into
                      evolution and function of enzymes from this superfamily.
                      Structural alignments with diverse
                      metallo-β-lactamase-fold-containing enzymes allowed the
                      identification of Protein Variable Regions accounting for
                      modulation of activity, specificity and oligomerization
                      patterns. Docking of different substrates within the active
                      sites revealed the basis for the crucial cofactor dependency
                      of this enzyme superfamily.},
      cin          = {NIC / JSC / IBI-7 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IMET-20090612},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / Forschergruppe
                      Gohlke $(hkf7_20200501)$ / DFG project 417919780 - Zentrum
                      für strukturelle Studien (417919780) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-5111 / $G:(DE-Juel1)hkf7_20200501$ /
                      G:(GEPRIS)417919780 / G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33514861},
      UT           = {WOS:000616759700006},
      doi          = {10.1038/s42003-021-01671-8},
      url          = {https://juser.fz-juelich.de/record/890392},
}