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FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.
|Title||FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Li Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang H-W, Ye S|
|Journal||Science (New York, N.Y.)|
|Date Published||2013 Jul 26|
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.