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@ARTICLE{Sgrignani:201299,
      author       = {Sgrignani, Jacopo and Magistrato, Alessandra and Dal
                      Peraro, Matteo and Vila, Alejandro J. and Carloni, Paolo and
                      Pierattelli, Roberta},
      title        = {{O}n the active site of mononuclear {B}1 metallo
                      β-lactamases: a computational study},
      journal      = {Journal of computer aided molecular design},
      volume       = {26},
      number       = {4},
      issn         = {1573-4951},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {FZJ-2015-03604},
      pages        = {425 - 435},
      year         = {2012},
      abstract     = {Metallo-β-lactamases (MβLs) are Zn(II)-based bacterial
                      enzymes that hydrolyze β-lactam antibiotics, hampering
                      their beneficial effects. In the most relevant subclass
                      (B1), X-ray crystallography studies on the enzyme from
                      Bacillus Cereus point to either two zinc ions in two metal
                      sites (the so-called ‘3H’ and ‘DCH’ sites) or a
                      single Zn(II) ion in the 3H site, where the ion is
                      coordinated by Asp120, Cys221 and His263 residues. However,
                      spectroscopic studies on the B1 enzyme from B. Cereus in the
                      mono-zinc form suggested the presence of the Zn(II) ion also
                      in the DCH site, where it is bound to an aspartate, a
                      cysteine, a histidine and a water molecule. A structural
                      model of this enzyme in its DCH mononuclear form, so far
                      lacking, is therefore required for inhibitor design and
                      mechanistic studies. By using force field based and mixed
                      quantum–classical (QM/MM) molecular dynamics (MD)
                      simulations of the protein in aqueous solution we
                      constructed such structural model. The geometry and the
                      H-bond network at the catalytic site of this model, in the
                      free form and in complex with two common β-lactam drugs, is
                      compared with experimental and theoretical findings of CphA
                      and the recently solved crystal structure of new B2 MβL
                      from Serratia fonticola (Sfh-I). These are MβLs from the B2
                      subclass, which features an experimentally well established
                      mono-zinc form, in which the Zn(II) is located in the DCH
                      site. From our simulations the εεδ and δεδ protomers
                      emerge as possible DCH mono-zinc reactive species, giving a
                      novel contribution to the discussion on the MβL reactivity
                      and to the drug design process.},
      cin          = {GRS / IAS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000303882200005},
      pubmed       = {pmid:22532071},
      doi          = {10.1007/s10822-012-9571-0},
      url          = {https://juser.fz-juelich.de/record/201299},
}