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@ARTICLE{Bggild:144095,
      author       = {Bøggild, A. and Sofos, N. and Andersen, K. and Feddersen,
                      A. and Easter, A. and Passmore, L. and Brodersen, D. and
                      DESY},
      title        = {{T}he {C}rystal {S}tructure of the {I}ntact {E}. coli
                      {R}el{BE} {T}oxin-{A}ntitoxin {C}omplex {P}rovides the
                      {S}tructural {B}asis for {C}onditional {C}ooperativity},
      journal      = {Structure},
      volume       = {20},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PHPPUBDB-25801},
      pages        = {1641},
      year         = {2012},
      abstract     = {The bacterial relBE locus encodes a toxin-antitoxin complex
                      in which the toxin, RelE, is capable of cleaving mRNA in the
                      ribosomal A site cotranslationally. The antitoxin, RelB,
                      both binds and inhibits RelE, and regulates transcription
                      through operator binding and conditional cooperativity
                      controlled by RelE. Here, we present the crystal structure
                      of the intact Escherichia coli RelB2E2 complex at 2.8 Å
                      resolution, comprising both the RelB-inhibited RelE and the
                      RelB dimerization domain that binds DNA. RelE and RelB
                      associate into a V-shaped heterotetrameric complex with the
                      ribbon-helix-helix (RHH) dimerization domain at the apex.
                      Our structure supports a model in which relO is optimally
                      bound by two adjacent RelB2E heterotrimeric units, and is
                      not compatible with concomitant binding of two RelB2E2
                      heterotetramers. The results thus provide a firm basis for
                      understanding the model of conditional cooperativity at the
                      molecular level.},
      keywords     = {Amino Acid Sequence / Bacterial Toxins: chemistry / Base
                      Sequence / Crystallography, X-Ray / DNA, Bacterial:
                      chemistry / Escherichia coli / Escherichia coli Proteins:
                      chemistry / Models, Molecular / Molecular Sequence Data /
                      Protein Binding / Protein Structure, Quaternary / Protein
                      Structure, Secondary / Protein Structure, Tertiary /
                      Bacterial Toxins (NLM Chemicals) / DNA, Bacterial (NLM
                      Chemicals) / Escherichia coli Proteins (NLM Chemicals) /
                      RelB protein, E coli (NLM Chemicals) / RelE protein, E coli
                      (NLM Chemicals)},
      cin          = {HASYLAB},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
      pnm          = {DORIS Beamline K1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.2-20130405},
      experiment   = {EXP:(DE-H253)D-K1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22981948},
      pmc          = {pmc:PMC3507626},
      UT           = {WOS:000309787900008},
      doi          = {10.1016/j.str.2012.08.017},
      url          = {https://bib-pubdb1.desy.de/record/144095},
}