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@ARTICLE{Shevchenko:185993,
      author       = {Shevchenko, Vitaly and Gushchin, Ivan and Polovinkin, V.
                      and Round, E. and Borshchevskiy, Valentin and Utrobin, P.
                      and Popov, A. and Balandin, Taras and Büldt, Georg and
                      Gordeliy, Valentin},
      title        = {{C}rystal {S}tructure of {E}scherichia coli-{E}xpressed
                      {H}aloarcula marismortui {B}acteriorhodopsin {I} in the
                      {T}rimeric {F}orm},
      journal      = {PLoS one},
      volume       = {9},
      number       = {12},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-00102},
      pages        = {e112873},
      year         = {2014},
      abstract     = {Bacteriorhodopsins are a large family of seven-helical
                      transmembrane proteins that function as light-driven proton
                      pumps. Here, we present the crystal structure of a new
                      member of the family, Haloarcula marismortui
                      bacteriorhodopsin I (HmBRI) D94N mutant, at the resolution
                      of 2.5 Å. While the HmBRI retinal-binding pocket and proton
                      donor site are similar to those of other archaeal proton
                      pumps, its proton release region is extended and contains
                      additional water molecules. The protein's fold is reinforced
                      by three novel inter-helical hydrogen bonds, two of which
                      result from double substitutions relative to Halobacterium
                      salinarum bacteriorhodopsin and other similar proteins.
                      Despite the expression in Escherichia coli and consequent
                      absence of native lipids, the protein assembles as a trimer
                      in crystals. The unique extended loop between the helices D
                      and E of HmBRI makes contacts with the adjacent protomer and
                      appears to stabilize the interface. Many lipidic hydrophobic
                      tail groups are discernible in the membrane region, and
                      their positions are similar to those of archaeal isoprenoid
                      lipids in the crystals of other proton pumps, isolated from
                      native or native-like sources. All these features might
                      explain the HmBRI properties and establish the protein as a
                      novel model for the microbial rhodopsin proton pumping
                      studies.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000346907200012},
      pubmed       = {pmid:25479443},
      doi          = {10.1371/journal.pone.0112873},
      url          = {https://juser.fz-juelich.de/record/185993},
}