% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Josts:442859,
      author       = {Josts, Inokentijs and Gao, Yunyun and Monteiro, Diana C. F.
                      and Niebling, Stephan and Nitsche, Julius and Veith,
                      Katharina and Gräwert, Tobias W. and Blanchet, Clement E.
                      and Schroer, Martin A. and Huse, Nils and Pearson, Arwen R.
                      and Svergun, Dmitri I. and Tidow, Henning},
      title        = {{S}tructural {K}inetics of {M}sb{A} {I}nvestigated by
                      {S}topped-{F}low {T}ime-{R}esolved {S}mall-{A}ngle {X}-{R}ay
                      {S}cattering},
      journal      = {Structure},
      volume       = {28},
      number       = {3},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {PUBDB-2020-03264},
      pages        = {348 - 354},
      year         = {2020},
      abstract     = {Recent structures of full-length ATP-binding cassette (ABC)
                      transporter MsbA in different states indicate large
                      conformational changes during the reaction cycle that
                      involve transient dimerization of its nucleotide-binding
                      domains (NBDs). However, a detailed molecular understanding
                      of the structural changes and associated kinetics of MsbA
                      upon ATP binding and hydrolysis is still missing. Here, we
                      employed time-resolved small-angle X-ray scattering,
                      initiated by stopped-flow mixing, to investigate the
                      kinetics and accompanying structural changes of NBD
                      dimerization (upon ATP binding) and subsequent dissociation
                      (upon ATP hydrolysis) in the context of isolated NBDs as
                      well as full-length MsbA in lipid nanodiscs. Our data
                      allowed us to structurally characterize the major states
                      involved in the process and determine time constants for NBD
                      dimerization and dissociation. In the full-length protein,
                      these structural transitions occur on much faster time
                      scales, indicating close-proximity effects and structural
                      coupling of the transmembrane domains with the NBDs.},
      cin          = {EMBL-User / CSSB-EMBL / EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814 /
                      I:(DE-H253)CSSB-EMBL-20141216 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (POF3-622) / DFG project 390715994 - EXC
                      2056: CUI: Advanced Imaging of Matter (390715994) / DFG
                      project 194651731 - EXC 1074: Hamburger Zentrum für
                      ultraschnelle Beobachtung (CUI): Struktur, Dynamik und
                      Kontrolle von Materie auf atomarer Skala (194651731)},
      pid          = {G:(DE-HGF)POF3-6G3 / G:(GEPRIS)390715994 /
                      G:(GEPRIS)194651731},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31899087},
      UT           = {WOS:000518466100010},
      doi          = {10.1016/j.str.2019.12.001},
      url          = {https://bib-pubdb1.desy.de/record/442859},
}