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	Mechanisms of actin filament severing and elongation by formins.
Journal, issue, pages	Nature, Year 2024
Publish date	Jun 6, 2024
Authors	Nicholas J Palmer / Kyle R Barrie / Roberto Dominguez /
PubMed Abstract	Humans express fifteen formins, playing crucial roles in actin-based processes, such as cytokinesis, cell motility, and mechanotransduction . However, the lack of structures bound to the actin ...Humans express fifteen formins, playing crucial roles in actin-based processes, such as cytokinesis, cell motility, and mechanotransduction . However, the lack of structures bound to the actin filament (F-actin) has been a major impediment to understanding formin function. While formins are known for their ability to nucleate and elongate F-actin , some formins can additionally depolymerize, sever, or bundle F-actin. Two mammalian formins, inverted formin-2 (INF2) and diaphanous-1 (Dia1), exemplify this diversity. INF2 displays potent severing activity but elongates weakly , whereas Dia1 has potent elongation activity but does not sever . Using cryo-electron microscopy (cryo-EM), we reveal five structural states of INF2 and two of Dia1 bound to the middle and barbed end of F-actin. INF2 and Dia1 bind differently to these sites, consistent with their distinct activities. The FH2 and WH2 domains of INF2 are positioned to sever F-actin, whereas Dia1 appears unsuited for severing. Structures also show how profilin-actin is delivered to the fast-growing barbed end, and how this is followed by a transition of the incoming monomer into the F-actin conformation and the release of profilin. Combined, the seven structures presented here provide step-by-step visualization of the mechanisms of F-actin severing and elongation by formins.
External links	Nature / PubMed:38843827
Methods	EM (single particle)
Resolution	2.86 - 4.38 Å
Structure data	EMDB-44009: INF2 at the Barbed End of F-actin, Consensus refinement Method: EM (single particle) / Resolution: 3.37 Å EMDB-44010: INF2 at the Barbed End of F-Actin, Leading WH2 focus refinement Method: EM (single particle) / Resolution: 4.17 Å EMDB-44011: INF2 at the Barbed End of F-Actin, Trailing WH2 focus refinement Method: EM (single particle) / Resolution: 4.09 Å 44012 9az4 EMDB-44012, PDB-9az4: INF2 at the Barbed End of F-Actin Method: EM (single particle) / Resolution: 3.37 Å 44018 9azp EMDB-44018, PDB-9azp: INF2 at the Barbed End of F-Actin with Incoming Profilin-Actin Method: EM (single particle) / Resolution: 3.79 Å 44019 9azq EMDB-44019, PDB-9azq: INF2 at the Barbed End of F-Actin with Incoming Actin Method: EM (single particle) / Resolution: 3.82 Å EMDB-44020: INF2 in the Middle of F-Actin, Up state consensus refinement Method: EM (single particle) / Resolution: 2.96 Å EMDB-44022: INF2 in the Middle of F-actin, Up state focus refinement for the static WH2 Method: EM (single particle) / Resolution: 3.18 Å EMDB-44023: INF2 in the Middle of Actin filament Method: EM (single particle) / Resolution: 2.86 Å EMDB-44024: INF2 at the Middle of F-Actin, Up state mobile FH2 local refinement Method: EM (single particle) / Resolution: 3.03 Å EMDB-44025: INF2 in the Middle of Actin Filament, Up state local refinement for static FH2 Method: EM (single particle) / Resolution: 2.87 Å 44026 9b03 EMDB-44026, PDB-9b03: INF2 in the Middle of F-Actin (Up state) Method: EM (single particle) / Resolution: 2.95 Å EMDB-44027: INF2 in the middle of F-actin, Down state consensus map Method: EM (single particle) / Resolution: 3.03 Å EMDB-44031: INF2 in the Middle of an Actin Filament, Down state actin local refinement Method: EM (single particle) / Resolution: 2.94 Å EMDB-44032: INF2 in the Middle of Actin Filament, Down state mobile FH2 local refinement Method: EM (single particle) / Resolution: 3.22 Å EMDB-44033: INF2 in the Middle of F-Actin, Down state static FH2 local refinement Method: EM (single particle) / Resolution: 3.05 Å 44045 9b0k EMDB-44045, PDB-9b0k: INF2 in the Middle of F-Actin (Down state) Method: EM (single particle) / Resolution: 3.03 Å 44099 9b27 EMDB-44099, PDB-9b27: Dia1 at the Barbed End of F-Actin Method: EM (single particle) / Resolution: 3.51 Å 44135 9b3d EMDB-44135: Dia1 in the Middle of F-actin PDB-9b3d: mDia1 in the middle of F-actin Method: EM (single particle) / Resolution: 3.41 Å EMDB-44943: INF2 in the middle of F-Actin, Focus refinement for mobile WH2 Method: EM (single particle) / Resolution: 3.26 Å EMDB-44948: INF2 in the Middle of F-actin, Up state mobile WH2 focus refinement Method: EM (single particle) / Resolution: 3.17 Å EMDB-44950: INF2 at the Barbed End of F-Actin, Local refinement for actin Method: EM (single particle) / Resolution: 3.3 Å EMDB-44951: INF2 at the Barbed End of F-Actin, Leading FH2 focused refinement Method: EM (single particle) / Resolution: 4.38 Å EMDB-44956: INF2 at the Barbed END with Incoming Profilin-Actin, Consensus refinement Method: EM (single particle) / Resolution: 3.55 Å EMDB-44958: INF2 at the Barbed End of F-Actin with Incoming Profilin-Actin, Actin local refinement Method: EM (single particle) / Resolution: 3.48 Å EMDB-44972: INF2 at the Barbed End of F-Actin with Incoming Actin, Actin local refinement Method: EM (single particle) / Resolution: 3.82 Å EMDB-44973: INF2 at the Barbed End of F-Actin with Incoming Actin, Consensus refinement Method: EM (single particle) / Resolution: 3.82 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate
Source	homo sapiens (human) oryctolagus cuniculus (rabbit) mus musculus (house mouse)
Keywords	CYTOSOLIC PROTEIN / Actin / Filament / Elongation / Ends / Formin / Severing