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	Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 117, Issue 3, Page 1478-1484, Year 2020
Publish date	Jan 21, 2020
Authors	Andrew R Huehn / Jeffrey P Bibeau / Anthony C Schramm / Wenxiang Cao / Enrique M De La Cruz / Charles V Sindelar /
PubMed Abstract	Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with ...Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subnanometer resolution maps of isolated, bound cofilin molecules and an actin-cofilactin boundary indicate that cofilin-induced actin conformational changes are local and limited to subunits directly contacting bound cofilin. An isolated, bound cofilin compromises longitudinal filament contacts of 1 protofilament, consistent with a single cofilin having filament-severing activity. An individual, bound phosphomimetic (S3D) cofilin with weak severing activity adopts a unique binding mode that does not perturb actin structure. Cofilin clusters disrupt both protofilaments, consistent with a higher severing activity at boundaries compared to single cofilin. Comparison of these structures indicates that this disruption is substantially greater at pointed end sides of cofilactin clusters than at the barbed end. These structures, with the distribution of bound cofilin clusters, suggest that maximum binding cooperativity is achieved when 2 cofilins occupy adjacent sites. These results reveal the structural origins of cooperative cofilin binding and actin filament severing.
External links	Proc Natl Acad Sci U S A / PubMed:31900364 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	3.4 - 9.2 Å
Structure data	20711 6vao EMDB-20711: Cryo-EM structure of cofilactin from partially cofilin-decorated actin filaments. PDB-6vao: Human cofilin-1 decorated actin filament Method: EM (helical sym.) / Resolution: 3.4 Å 20719 6vau EMDB-20719: Bare actin from partially cofilin-decorated actin filaments PDB-6vau: Bare actin filament from a partially cofilin-decorated sample Method: EM (helical sym.) / Resolution: 3.5 Å 20721 6uby EMDB-20721, PDB-6uby: Isolated cofilin bound to an actin filament Method: EM (single particle) / Resolution: 7.5 Å 20724 6uc0 EMDB-20724, PDB-6uc0: Isolated S3D-cofilin bound to an actin filament Method: EM (single particle) / Resolution: 7.5 Å 20726 6uc4 EMDB-20726, PDB-6uc4: Barbed end side of a cofilactin cluster Method: EM (single particle) / Resolution: 9.2 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate
Source	oryctolagus cuniculus (rabbit) homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / Cytoskeleton