FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.

TitleFtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.
Publication TypeJournal Article
Year of Publication2013
AuthorsLi Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang H-W, Ye S
JournalScience (New York, N.Y.)
Volume341
Issue6144
Pagination392-5
Date Published2013 Jul 26
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.

DOI10.3348/kjr.2013.14.4.581
Alternate JournalScience