National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01HL144131
United States
Citation
Journal: Sci Adv / Year: 2022 Title: Molecular architecture of the human caveolin-1 complex. Authors: Jason C Porta / Bing Han / Alican Gulsevin / Jeong Min Chung / Yelena Peskova / Sarah Connolly / Hassane S Mchaourab / Jens Meiler / Erkan Karakas / Anne K Kenworthy / Melanie D Ohi / Abstract: Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin ...Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function.
History
Deposition
Sep 26, 2021
Deposition site: RCSB / Processing site: RCSB
Revision 1.0
May 25, 2022
Provider: repository / Type: Initial release
Revision 1.1
Jun 5, 2024
Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Average exposure time: 6 sec. / Electron dose: 55.5 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 984
Image scans
Sampling size: 0.98 µm / Width: 3838 / Height: 3710 / Movie frames/image: 30 / Used frames/image: 1-30
Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 60615 / Algorithm: BACK PROJECTION / Num. of class averages: 1 / Symmetry type: POINT
Atomic model building
B value: 37.8 / Protocol: AB INITIO MODEL / Space: REAL / Target criteria: Correlation coefficient
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
ELECTRONMICROSCOPY
f_bond_d
0.002
11990
ELECTRONMICROSCOPY
f_angle_d
0.432
16335
ELECTRONMICROSCOPY
f_dihedral_angle_d
3.356
1507
ELECTRONMICROSCOPY
f_chiral_restr
0.043
1859
ELECTRONMICROSCOPY
f_plane_restr
0.003
1991
+
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