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	Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.
Journal, issue, pages	Nat Struct Mol Biol, Year 2024
Publish date	Aug 16, 2024
Authors	Benedikt Junglas / Esther Hudina / Philipp Schönnenbeck / Ilona Ritter / Anja Heddier / Beatrix Santiago-Schübel / Pitter F Huesgen / Dirk Schneider / Carsten Sachse /
PubMed Abstract	Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) ...Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) has been identified as a member of the ESCRT-III superfamily, and PspA homo-oligomerizes to form rod-shaped assemblies. As observed for eukaryotic ESCRT-III, PspA forms tubular assemblies of varying diameters. Using electron cryo-electron microscopy, we determined 61 Synechocystis PspA structures and observed in molecular detail how the structural plasticity of PspA rods is mediated by conformational changes at three hinge regions in the monomer and by the fixed and changing molecular contacts between protomers. Moreover, we reduced and increased the structural plasticity of PspA rods by removing the loop connecting helices α3/α4 and the addition of nucleotides, respectively. Based on our analysis of PspA-mediated membrane remodeling, we suggest that the observed mode of structural plasticity is a prerequisite for the biological function of ESCRT-III members.
External links	Nat Struct Mol Biol / PubMed:39152237
Methods	EM (helical sym.)
Resolution	3.8 - 6.9 Å
Structure data	15489 8akq EMDB-15489, PDB-8akq: 180 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 4.1 Å 15490 8akr EMDB-15490, PDB-8akr: 200 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 3.8 Å 15491 8aks EMDB-15491, PDB-8aks: 215 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 3.9 Å 15492 8akt EMDB-15492, PDB-8akt: 235 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 4.4 Å 15493 8aku EMDB-15493, PDB-8aku: 250 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 4.5 Å 15494 8akv EMDB-15494, PDB-8akv: 270 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 4.4 Å 15495 8akw EMDB-15495, PDB-8akw: 280 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 5.4 Å 15496 8akx EMDB-15496, PDB-8akx: 305 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 6.6 Å 15497 8aky EMDB-15497, PDB-8aky: 290 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 4.7 Å 15498 8akz EMDB-15498, PDB-8akz: 320 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 6.9 Å 15499 8al0 EMDB-15499, PDB-8al0: 365 A SynPspA rod after incubation with ATP Method: EM (helical sym.) / Resolution: 6.9 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM
Source	synechocystis sp. pcc 6803 (bacteria)
Keywords	LIPID BINDING PROTEIN / Nucleotide binding / Helical assembly / ESCRT-III fold / Membrane remodeling