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	The cohesin ATPase cycle is mediated by specific conformational dynamics and interface plasticity of SMC1A and SMC3 ATPase domains.
Journal, issue, pages	Cell Rep, Vol. 43, Issue 9, Page 114656, Year 2024
Publish date	Sep 24, 2024
Authors	Marina Vitoria Gomes / Pauline Landwerlin / Marie-Laure Diebold-Durand / Tajith B Shaik / Alexandre Durand / Edouard Troesch / Chantal Weber / Karl Brillet / Marianne Victoria Lemée / Christophe Decroos / Ludivine Dulac / Pierre Antony / Erwan Watrin / Eric Ennifar / Christelle Golzio / Christophe Romier /
PubMed Abstract	Cohesin is key to eukaryotic genome organization and acts throughout the cell cycle in an ATP-dependent manner. The mechanisms underlying cohesin ATPase activity are poorly understood. Here, we ...Cohesin is key to eukaryotic genome organization and acts throughout the cell cycle in an ATP-dependent manner. The mechanisms underlying cohesin ATPase activity are poorly understood. Here, we characterize distinct steps of the human cohesin ATPase cycle and show that the SMC1A and SMC3 ATPase domains undergo specific but concerted structural rearrangements along this cycle. Specifically, whereas the proximal coiled coil of the SMC1A ATPase domain remains conformationally stable, that of the SMC3 displays an intrinsic flexibility. The ATP-dependent formation of the heterodimeric SMC1A/SMC3 ATPase module (engaged state) favors this flexibility, which is counteracted by NIPBL and DNA binding (clamped state). Opening of the SMC3/RAD21 interface (open-engaged state) stiffens the SMC3 proximal coiled coil, thus constricting together with that of SMC1A the ATPase module DNA-binding chamber. The plasticity of the ATP-dependent interface between the SMC1A and SMC3 ATPase domains enables these structural rearrangements while keeping the ATP gate shut. VIDEO ABSTRACT.
External links	Cell Rep / PubMed:39240714
Methods	EM (single particle) / X-ray diffraction
Resolution	1.36 - 4.4 Å
Structure data	17331 8p0a EMDB-17331, PDB-8p0a: Human Cohesin ATPase module Method: EM (single particle) / Resolution: 3.67 Å 17820 8pq5 EMDB-17820, PDB-8pq5: Human Cohesin ATPase module with an open DNA exit gate Method: EM (single particle) / Resolution: 4.4 Å PDB-8ro6: Human cohesin SMC1A-HD(longCC)/RAD21-C complex - Apo closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-8ro7: Human cohesin SMC1A-HD(longCC)/RAD21-C complex - Open/closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 2.0929 Å PDB-8ro8: Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Apo closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 1.902 Å PDB-8ro9: Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Open/closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 1.767 Å PDB-8roa: Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - ADP-bound conformation Method: X-RAY DIFFRACTION / Resolution: 2.4355 Å PDB-8rob: Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation Method: X-RAY DIFFRACTION / Resolution: 2.5019 Å PDB-8roc: Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - Apo closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 1.85 Å PDB-8rod: Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - Open/closed P-loop conformation Method: X-RAY DIFFRACTION / Resolution: 1.5 Å PDB-8roe: Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ADP-bound conformation Method: X-RAY DIFFRACTION / Resolution: 1.36 Å PDB-8rof: Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ADP-Mg-bound conformation Method: X-RAY DIFFRACTION / Resolution: 1.65 Å PDB-8rog: Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation Method: X-RAY DIFFRACTION / Resolution: 1.94 Å PDB-8roh: Human cohesin SMC3-HD(EQ)/RAD21-N complex - Apo conformation Method: X-RAY DIFFRACTION / Resolution: 2.6 Å PDB-8roi: Human cohesin SMC3-HD(EQ)/RAD21-N complex - ADP-bound conformation Method: X-RAY DIFFRACTION / Resolution: 2.45 Å PDB-8roj: Human cohesin SMC3-HD/RAD21-N complex - ADP-Mg-bound conformation Method: X-RAY DIFFRACTION / Resolution: 3 Å PDB-8rok: Human cohesin SMC3-HD(EQ)/RAD21-N complex - ATP-Mg-bound conformation - Form 1 Method: X-RAY DIFFRACTION / Resolution: 2.25 Å PDB-8rol: Human cohesin SMC3-HD(EQ)/RAD21-N complex - ATP-Mg-bound conformation - Form 2 Method: X-RAY DIFFRACTION / Resolution: 3.11 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-B3P: 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH bufferYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM ChemComp-SO4: SULFATE ION ChemComp-GOL: GLYCEROL
Source	homo sapiens (human)
Keywords	DNA BINDING PROTEIN / 3D genome organization / Chromatin / Cohesin / ATPase activity / ATPase cycle / Cell cycle / DNA binding / NUCLEAR PROTEIN