4N1A

Thermomonospora curvata EccC (ATPases 2 and 3) in complex with a signal sequence peptide

4N1A の概要

• エントリーDOI: 10.2210/pdb4n1a/pdb
• 分子名称: Cell divisionFtsK/SpoIIIE, Uncharacterized protein, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: atpase, protein binding-protein binding complex, protein binding/protein binding
• 由来する生物種: Thermomonospora curvata; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 272732.65

構造登録者

Dovala, D.L.,Bendebury, A.,Cox, J.S.,Stroud, R.M.,Rosenberg, O.S. (登録日: 2013-10-03, 公開日: 2015-02-11, 最終更新日: 2024-02-28)

主引用文献

Rosenberg, O.S.,Dovala, D.,Li, X.,Connolly, L.,Bendebury, A.,Finer-Moore, J.,Holton, J.,Cheng, Y.,Stroud, R.M.,Cox, J.S.
Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion.
Cell(Cambridge,Mass.), 161:501-512, 2015

PubMed Abstract: Mycobacterium tuberculosis and Staphylococcus aureus secrete virulence factors via type VII protein secretion (T7S), a system that intriguingly requires all of its secretion substrates for activity. To gain insights into T7S function, we used structural approaches to guide studies of the putative translocase EccC, a unique enzyme with three ATPase domains, and its secretion substrate EsxB. The crystal structure of EccC revealed that the ATPase domains are joined by linker/pocket interactions that modulate its enzymatic activity. EsxB binds via its signal sequence to an empty pocket on the C-terminal ATPase domain, which is accompanied by an increase in ATPase activity. Surprisingly, substrate binding does not activate EccC allosterically but, rather, by stimulating its multimerization. Thus, the EsxB substrate is also an integral T7S component, illuminating a mechanism that helps to explain interdependence of substrates, and suggests a model in which binding of substrates modulates their coordinate release from the bacterium.

PubMed: 25865481
DOI: 10.1016/j.cell.2015.03.040

実験手法

X-RAY DIFFRACTION (3.24 Å)