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@ARTICLE{Gmelin:59154,
      author       = {Gmelin, W. and Zeth, K. and Efremov, R. and Heberle, J. and
                      Tittor, J. and Oesterhelt, D.},
      title        = {{T}he {C}rystal {S}tructure of the {L}1 {I}ntermediate of
                      {H}alorhodopsin at 1.9 Å {R}esolution},
      journal      = {Photochemistry and photobiology},
      volume       = {83},
      issn         = {0031-8655},
      address      = {Malden, Mass.},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-59154},
      pages        = {369 - 377},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The mutant T203V of the light driven chloride pump
                      halorhodopsin from Halobacterium salinarum was crystallized
                      and the X-ray structure was solved at 1.6 angstroms
                      resolution. The T203V structure turned out to be nearly
                      identical to the wild type protein with a root mean square
                      deviation of 0.43 angstroms for the carbon alpha atoms of
                      the protein backbone. Two chloride binding (CB) sites were
                      demonstrated by a substitution of chloride with bromide and
                      an analysis of anomalous difference Fourier maps. The CB1
                      site was found at the same position as in the wild type
                      structure. In addition, a second chloride binding site CB2
                      was identified around Q105 due to higher resolution in the
                      mutant crystal. As T203V showed a 10 times slower decay of
                      its photocycle intermediate L, this intermediate could be
                      trapped with an occupancy of $60\%$ upon illumination at
                      room temperature and subsequent cooling to 120 degrees K.
                      Fourier transform infrared spectroscopy clearly identified
                      the crystal to be trapped in the L1 intermediate state and
                      the X-ray structure was solved to 1.9 angstroms resolution.
                      In this intermediate, the chloride moved by 0.3 angstroms
                      within binding site CB1 as indicated by peaks in difference
                      Fourier density maps. The chloride in the second binding
                      site CB2 remained unchanged. Thus, intraproteinous chloride
                      translocation from the extracellular to the cytoplasmic part
                      of the protein must occur in reaction steps following the L1
                      intermediate in the catalytic cycle of halorhodopsin.},
      keywords     = {Amino Acid Substitution / Binding Sites / Chlorides:
                      chemistry / Crystallography, X-Ray / Halobacterium
                      salinarum: chemistry / Halobacterium salinarum: genetics /
                      Halobacterium salinarum: radiation effects / Halorhodopsins:
                      chemistry / Halorhodopsins: genetics / Halorhodopsins:
                      radiation effects / Models, Molecular / Mutagenesis,
                      Site-Directed / Photochemistry / Chlorides (NLM Chemicals) /
                      Halorhodopsins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17117890},
      UT           = {WOS:000245658000023},
      doi          = {10.1562/2006-06-23-RA-947},
      url          = {https://juser.fz-juelich.de/record/59154},
}