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@ARTICLE{Dubey:570307,
      author       = {Dubey, Badri Nath and Shyp, Viktoriya and Fucile, Geoffrey
                      and Sondermann, Holger and Jenal, Urs and Schirmer, Tilman},
      title        = {{M}utant structure of metabolic switch protein in complex
                      with monomeric c-di-{GMP} reveals a potential mechanism of
                      protein mediated ligand dimerization},
      journal      = {Scientific reports},
      volume       = {13},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2023-00670},
      pages        = {2727},
      year         = {2023},
      abstract     = {Bacterial second messengers c-di-GMP and (p)ppGpp have
                      broad functional repertoires ranging from growth and cell
                      cycle control to the regulation of biofilm formation and
                      virulence. The recent identification of SmbA, an effector
                      protein from Caulobacter crescentus that is jointly targeted
                      by both signaling molecules, has opened up studies on how
                      these global bacterial networks interact. C-di-GMP and
                      (p)ppGpp compete for the same SmbA binding site, with a
                      dimer of the c-di-GMP inducing a conformational change that
                      involves loop 7 of the protein thats leads to downstream
                      signaling. Here, we report a crystal structure of a partial
                      loop 7 deletion mutant, SmbA∆loop in complex with c-di-GMP
                      determined at 1.4 Å resolution. SmbA∆loop binds monomeric
                      c-di-GMP indicating that loop 7 is required for c-di-GMP
                      dimerization. Thus the complex probably represents the first
                      step of consecutive c-di-GMP binding to form intercalated
                      dimer as has been observed in wild-type SmbA. . Considering
                      the prevalence of intercalated c-di-GMP molecules observed
                      bound to proteins, the proposed mechanism may be generally
                      applicable to protein-mediated c-di-GMP dimerization.
                      Notably, in the crystal, SmbA∆loop forms a 2-fold
                      symmetric dimer via isologous interactions with the two
                      symmetric halves of c-di-GMP. Structural comparisons of
                      SmbA∆loop with wild-type SmbA in complex with dimeric
                      c-di-GMP or ppGpp support the idea that loop 7 is critical
                      for SmbA function by interacting with downstream partners.
                      Our results also underscore the flexibility of c-di-GMP, to
                      allow binding to the symmetric SmbA∆loop dimer interface.
                      It is envisaged that such isologous interactions of c-di-GMP
                      could be observed in hitherto unrecognized targets.},
      cin          = {CSSB-DESY-HS},
      ddc          = {600},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P03-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36810577},
      UT           = {WOS:001003439800022},
      doi          = {10.1038/s41598-023-29110-0},
      url          = {https://bib-pubdb1.desy.de/record/570307},
}