Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A

  • Baisen Zeng
  • , Tung Chung Mou
  • , Tzanko I. Doukov
  • , Andrea Steiner
  • , Wenxi Yu
  • , Makaia Papasergi-Scott
  • , Gregory G. Tall
  • , Franz Hagn
  • , Stephen R. Sprang

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Zeng et al. use X-ray crystallography and small-angle scattering, in conjunction with NMR spectroscopy, to reveal the structure of and dynamics of the G protein chaperone and activator Ric-8A and probe its interaction with the G protein alpha subunit i1.

Original languageEnglish
Pages (from-to)1137-1147.e5
JournalStructure
Volume27
Issue number7
DOIs
StatePublished - Jul 2 2019

Funding

We thank Drs. Wuxian Shi and Martin Fuchs at the National Synchrotron Light Source II (NSLS II) FMX beamline, and the staff at Advanced Photon Source (APS)/Structural Biology Center (SBC)-CAT 19-BM and Stanford Synchrotron Laboratory (SSRL) beamline 9-1 for excellent assistance with X-ray crystallographic data collection and from Dr. Tsutomu Matsui at the SSRL 4-2 beamline and Cindee Yates-Hansen for assistance with FPLC-SAXS data collection, and Dr. Celestine Thomas for his assistance during earlier phases of the project. The FMX (17-ID-2) beamline is supported by NIH grant P41GM111244 and the Department of Energy (DOE), KP1605010 . SSRL is supported by the DOE under contract no. DE-AC02-76SF00515. The SSRL Structural Molecular Biology Program is supported by the DOE and by NIH grant P41GM103393 . The SBC-CAT at APS is supported by DOE under contract DE-AC02-06CH11357. This research was supported by NIH R01GM105993 (to S.R.S.), the Helmholtz Society and the Helmholtz Zentrum München grant VH-NG-1039 and DFG grant HA6105/3-1 (to F.H.), NIH R01-GM088242 (to G.G.T.), RHHMI “Med-into-Grad” Fellowship, NIH T32-GM06841 and pre-doctoral fellowship from the PhRMA Foundation (to M.P.-S.). The Macromolecular X-ray Diffraction Core at the University of Montana Center for Biomolecular Structure and Dynamics is supported by NIH COBRE award P20GM103546 . We thank Drs. Wuxian Shi and Martin Fuchs at the National Synchrotron Light Source II (NSLS II) FMX beamline, and the staff at Advanced Photon Source (APS)/Structural Biology Center (SBC)-CAT 19-BM and Stanford Synchrotron Laboratory (SSRL) beamline 9-1 for excellent assistance with X-ray crystallographic data collection and from Dr. Tsutomu Matsui at the SSRL 4-2 beamline and Cindee Yates-Hansen for assistance with FPLC-SAXS data collection, and Dr. Celestine Thomas for his assistance during earlier phases of the project. The FMX (17-ID-2) beamline is supported by NIH grant P41GM111244 and the Department of Energy (DOE), KP1605010. SSRL is supported by the DOE under contract no. DE-AC02-76SF00515. The SSRL Structural Molecular Biology Program is supported by the DOE and by NIH grant P41GM103393. The SBC-CAT at APS is supported by DOE under contract DE-AC02-06CH11357. This research was supported by NIH R01GM105993 (to S.R.S.), the Helmholtz Society and the Helmholtz Zentrum München grant VH-NG-1039 and DFG grant HA6105/3-1 (to F.H.), NIH R01-GM088242 (to G.G.T.), RHHMI “Med-into-Grad” Fellowship, NIH T32-GM06841 and pre-doctoral fellowship from the PhRMA Foundation (to M.P.-S.). The Macromolecular X-ray Diffraction Core at the University of Montana Center for Biomolecular Structure and Dynamics is supported by NIH COBRE award P20GM103546. S.R.S. T.-C.M. B.Z. and F.H. designed the research. B.Z. T.-C.M. A.S. and W.Y. performed the research. M.P.-S. and G.G.T. provided the data before publication. T.I.D. contributed technical guidance. S.R.S. T.-C.M. F.H. and A.S. analyzed the data and S.R.S. wrote the paper with contributions from T.-C.M. B.Z. F.H. and G.G.T. The authors declare no competing interests.

FundersFunder number
P41GM111244
P41GM103393, DE-AC02-06CH11357, R01GM105993, KP1605010, DE-AC02-76SF00515
R01GM088242
P20GM103546
HA6105/3-1, T32-GM06841, R01-GM088242
Helmholtz Zentrum München - German Research Center for Environmental HealthVH-NG-1039

    Keywords

    • X-ray crystallography
    • guanine nucleotide exchange factor
    • heteronuclear nuclear magnetic resonance
    • heterotrimeric G protein
    • molecular chaperone
    • protein dynamics
    • protein structure
    • small-angle X-ray scattering

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