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@ARTICLE{Golub:873376,
      author       = {Golub, Maksym and Moldenhauer, Marcus and Schmitt,
                      Franz-Josef and Feoktystov, Artem and Mändar, Hugo and
                      Maksimov, Eugene and Friedrich, Thomas and Pieper, Jörg},
      title        = {{S}olution {S}tructure and {C}onformational {F}lexibility
                      in the {A}ctive {S}tate of the {O}range {C}arotenoid
                      {P}rotein: {P}art {I}. {S}mall-{A}ngle {S}cattering},
      journal      = {The journal of physical chemistry / B B, Condensed matter,
                      materials, surfaces, interfaces $\&$ biophysical},
      volume       = {123},
      number       = {45},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-00688},
      pages        = {9525 - 9535},
      year         = {2019},
      abstract     = {Orange carotenoid proteins (OCPs) are photoswitchable
                      macromolecules playing an important role in nonphotochemical
                      quenching of excess energy in cyanobacterial light
                      harvesting. Upon absorption of a blue photon (450–500 nm),
                      OCPs undergo a structural change from the ground state OCPO
                      to the active state OCPR, but high-resolution structures of
                      the active state OCPR are not yet available. Here, we use
                      small-angle scattering methods combined with simulation
                      tools to determine low-resolution structures of the active
                      state at low protein concentrations via two approaches:
                      first, directly by in situ illumination of wild-type OCP
                      achieving a turnover to the active state of $>90\%$ and
                      second, by using the mutant OCPW288A anticipated to mimic
                      the active state structure. Data fits assuming the shape of
                      an ellipsoid yield three ellipsoidal radii of about 9, 29,
                      and 51 ± 1 Å, in the case of the ground state OCPO. In the
                      active state, however, the molecule becomes somewhat
                      narrower with the two smaller radii being 9 and only 19 ± 3
                      Å, while the third dimension of the ellipsoid is
                      significantly elongated to 85–92 ± 5 Å. Reconstitutions
                      of the active state structure corroborate that OCPR is
                      significantly elongated compared to the ground state OCPO
                      and characterized by a separation of the N-terminal and
                      C-terminal domains with unfolded N-terminal extension. By
                      direct comparison of small-angle scattering data, we
                      directly show that the mutant OCPW288A can be used as a
                      structural analogue of the active state OCPR. The
                      small-angle experiments are repeated for OCPO and the mutant
                      OCPW288A at high protein concentrations of 50–65 mg/mL
                      required for neutron spectroscopy investigating the
                      molecular dynamics of OCP (see accompanying paper). The
                      results reveal that the OCPO and OCPW288A samples for
                      dynamics experiments are preferentially dimeric and widely
                      resemble the structures of the ground and active states of
                      OCP, respectively. This enables us to properly characterize
                      the molecular dynamics of both states of OCP in the
                      accompanying paper.},
      cin          = {JCNS-FRM-II / JCNS-2 / MLZ},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-2-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31556613},
      UT           = {WOS:000497259800002},
      doi          = {10.1021/acs.jpcb.9b05071},
      url          = {https://juser.fz-juelich.de/record/873376},
}