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Science. 2013 Jul 26;341(6144):392-5. doi: 10.1126/science.1239248.

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

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1
Life Sciences Institute, Zhejiang University, Hangzhou, 310058 Zhejiang, P.R. China.

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.

PMID:
23888039
PMCID:
PMC3816583
DOI:
10.1126/science.1239248
[Indexed for MEDLINE]
Free PMC Article
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