Science. 2013 Jul 26;341(6144):392-5.

Ying Li, Jen Hsin, Lingyun Zhao, Yiwen Cheng, Weina Shang, Kerwyn Casey Huang, Hong-Wei Wang, Sheng Ye*

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.

Text link：http://www.sciencemag.org/content/341/6144/392.full