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@ARTICLE{Genna:841290,
      author       = {Genna, Vito and Colombo, Matteo and De Vivo, Marco and
                      Marcia, Marco},
      title        = {{S}econd-{S}hell {B}asic {R}esidues {E}xpand the
                      {T}wo-{M}etal-{I}on {A}rchitecture of {DNA} and {RNA}
                      {P}rocessing {E}nzymes},
      journal      = {Structure},
      volume       = {26},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2017-08381},
      pages        = {40-50},
      year         = {2018},
      abstract     = {Synthesis and scission of phosphodiester bonds in DNA and
                      RNA regulate vital processes within the cell. Enzymes that
                      catalyze these reactions operate mostly via the recognized
                      two-metal-ion mechanism. Our analysis reveals that basic
                      amino acids and monovalent cations occupy structurally
                      conserved positions nearby the active site of many
                      two-metal-ion enzymes for which high-resolution (<3 Å)
                      structures are known, including DNA and RNA polymerases,
                      nucleases such as Cas9, and splicing ribozymes. Integrating
                      multiple-sequence and structural alignments with molecular
                      dynamics simulations, electrostatic potential maps, and
                      mutational data, we found that these elements always
                      interact with the substrates, suggesting that they may play
                      an active role for catalysis, in addition to their
                      electrostatic contribution. We discuss possible mechanistic
                      implications of this expanded two-metal-ion architecture,
                      including inferences on medium-resolution cryoelectron
                      microscopy structures. Ultimately, our analysis may inspire
                      future experiments and strategies for enzyme engineering or
                      drug design to modulate nucleic acid processing.},
      cin          = {IAS-5 / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {574 - Theory, modelling and simulation (POF3-574)},
      pid          = {G:(DE-HGF)POF3-574},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29225080},
      UT           = {WOS:000419101700007},
      doi          = {10.1016/j.str.2017.11.008},
      url          = {https://juser.fz-juelich.de/record/841290},
}