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-Structure paper
タイトル | Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Year 2024 |
掲載日 | 2024年8月16日 |
著者 | Benedikt Junglas / Esther Hudina / Philipp Schönnenbeck / Ilona Ritter / Anja Heddier / Beatrix Santiago-Schübel / Pitter F Huesgen / Dirk Schneider / Carsten Sachse / |
PubMed 要旨 | 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. |
リンク | Nat Struct Mol Biol / PubMed:39152237 |
手法 | EM (らせん対称) |
解像度 | 3.8 - 6.9 Å |
構造データ | EMDB-15489, PDB-8akq: EMDB-15490, PDB-8akr: EMDB-15491, PDB-8aks: EMDB-15492, PDB-8akt: EMDB-15493, PDB-8aku: EMDB-15494, PDB-8akv: EMDB-15495, PDB-8akw: EMDB-15496, PDB-8akx: EMDB-15497, PDB-8aky: EMDB-15498, PDB-8akz: EMDB-15499, PDB-8al0: |
化合物 | ChemComp-ADP: |
由来 |
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キーワード | LIPID BINDING PROTEIN / Nucleotide binding / Helical assembly / ESCRT-III fold / Membrane remodeling |