Journal
SCIENCE
Volume 341, Issue 6144, Pages 392-395Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1239248
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Funding
- National Natural Science Foundation of China [31070661]
- Ministry of Science and Technology [2011CB910500, 2010CB912401, 2012CB966600]
- Natural Science Foundation of Zhejiang Province [R2100439]
- Specialized Research Fund for the Doctoral Program of Higher Education [20110101110122]
- Fundamental Research Funds for the Central Universities
- Research Funds of the Tsinghua-Peking Center for Life Sciences
- NIH [DP2OD006466]
- Stanford University School of Medicine
- NIH Ruth L. Kirschstein National Research Service Award [1F32GM100677-01A1]
- National Science Foundation of China [31090360]
- NSF [OCI-1053575]
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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.
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