Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Scaffold subunits support associated subunit assembly in the ciliary nexin-dynein regulatory complex.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 46, Page 23152-23162, Year 2019
Publish date	Nov 12, 2019
Authors	Long Gui / Kangkang Song / Douglas Tritschler / Raqual Bower / Si Yan / Aguang Dai / Katherine Augspurger / Jason Sakizadeh / Magdalena Grzemska / Thomas Ni / Mary E Porter / Daniela Nicastro /
PubMed Abstract	The nexin-dynein regulatory complex (N-DRC) in motile cilia and flagella functions as a linker between neighboring doublet microtubules, acts to stabilize the axonemal core structure, and serves as a ...The nexin-dynein regulatory complex (N-DRC) in motile cilia and flagella functions as a linker between neighboring doublet microtubules, acts to stabilize the axonemal core structure, and serves as a central hub for the regulation of ciliary motility. Although the N-DRC has been studied extensively using genetic, biochemical, and structural approaches, the precise arrangement of the 11 (or more) N-DRC subunits remains unknown. Here, using cryo-electron tomography, we have compared the structure of wild-type flagella to that of strains with specific DRC subunit deletions or rescued strains with tagged DRC subunits. Our results show that DRC7 is a central linker subunit that helps connect the N-DRC to the outer dynein arms. DRC11 is required for the assembly of DRC8, and DRC8/11 form a subcomplex in the proximal lobe of the linker domain that is required to form stable contacts to the neighboring B-tubule. Gold labeling of tagged subunits determines the precise locations of the previously ambiguous N terminus of DRC4 and C terminus of DRC5. DRC4 is now shown to contribute to the core scaffold of the N-DRC. Our results reveal the overall architecture of N-DRC, with the 3 subunits DRC1/2/4 forming a core complex that serves as the scaffold for the assembly of the "functional subunits," namely DRC3/5-8/11. These findings shed light on N-DRC assembly and its role in regulating flagellar beating.
External links	Proc Natl Acad Sci U S A / PubMed:31659045 / PubMed Central
Methods	EM (subtomogram averaging)
Resolution	26.0 - 40.0 Å
Structure data	EMDB-20338: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas wild type axonemes Method: EM (subtomogram averaging) / Resolution: 27.0 Å EMDB-20339: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas drc7 axonemes Method: EM (subtomogram averaging) / Resolution: 28.0 Å EMDB-20340: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas drc11 axonemes Method: EM (subtomogram averaging) / Resolution: 26.0 Å EMDB-20341: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas SNAP-DRC4 axonemes, labeled with streptavidin-nanogold Method: EM (subtomogram averaging) / Resolution: 35.0 Å EMDB-20821: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas DRC5-SNAP axonemes, labeled with streptavidin-nanogold Method: EM (subtomogram averaging) / Resolution: 40.0 Å
Source	Chlamydomonas reinhardtii (plant)