| 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
|
| リソース情報 |
| 原核生物(大腸菌) |
BL21(DE3) |
