Download MendeleyFtsZ protofilaments use a hinge-opening mechanism for constrictive force generation
Li, Y., Hsin, J., Zhao, L., Cheng, Y., Shang, W., Huang, K.C., Wang, H.W., Ye, S.(2013) Science 341: 392-395
- PubMed: 23888039
- DOI: https://doi.org/10.1126/science.1239248
- Primary Citation of Related Structures:
4KWE - PubMed Abstract:
The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a structure at the division site termed the "Z ring". During cytokinesis, the Z ring exerts a constrictive force on the membrane by using the chemical energy of guanosine triphosphate hydrolysis. However, the structural basis of this constriction remains unresolved. Here, we present the crystal structure of a guanosine diphosphate-bound Mycobacterium tuberculosis FtsZ protofilament, which exhibits a curved conformational state. The structure reveals a longitudinal interface that is important for function. The protofilament curvature highlights a hydrolysis-dependent conformational switch at the T3 loop that leads to longitudinal bending between subunits, which could generate sufficient force to drive cytokinesis.
Organizational Affiliation:
Life Sciences Institute, Zhejiang University, Hangzhou, 310058 Zhejiang, P.R. China.
