論文 - 詳細
| RRC ID | 50592 |
|---|---|
| 著者 | Kamada K, Su'etsugu M, Takada H, Miyata M, Hirano T. |
| タイトル | Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts. |
| ジャーナル | Structure |
| Abstract |
The SMC-ScpAB complex plays a crucial role in chromosome organization and segregation in many bacteria. It is composed of a V-shaped SMC dimer and an ScpAB subcomplex that bridges the two Structural Maintenance of Chromosomes (SMC) head domains. Despite its functional significance, the mechanistic details of SMC-ScpAB remain obscure. Here we provide evidence that ATP-dependent head-head engagement induces a lever movement of the SMC neck region, which might help to separate juxtaposed coiled-coil arms. Binding of the ScpA N-terminal domain (NTD) to the SMC neck region is negatively regulated by the ScpB C-terminal domain. Mutations in the ScpA NTD compromise this regulation and profoundly affect the overall shape of the complex. The SMC hinge domain is structurally relaxed when free from coiled-coil juxtaposition. Taken together, we propose that the structural parts of SMC-ScpAB are subjected to the balance between constraint and relaxation, cooperating to modulate dynamic conformational changes of the whole complex. |
| 巻・号 | 25(4) |
| ページ | 603-616.e4 |
| 公開日 | 2017-4-4 |
| DOI | 10.1016/j.str.2017.02.008 |
| PII | S0969-2126(17)30039-4 |
| PMID | 28286005 |
| MeSH | Binding Sites Cell Cycle Proteins / chemistry* Cell Cycle Proteins / genetics Cell Cycle Proteins / metabolism* Crystallography, X-Ray Models, Molecular Mutation Protein Binding Protein Multimerization |
| IF | 4.862 |
| 引用数 | 22 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 4 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 原核生物(大腸菌) | BL21(DE3) |