ZapA family
| ZapA | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The crystal structure of the bacterial cell division protein ZapA | |||||||||
| Identifiers | |||||||||
| Symbol | ZapA | ||||||||
| Pfam | PF05164 | ||||||||
| InterPro | IPR007838 | ||||||||
| SCOP2 | 1t3u / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the ZapA protein family is a group of related proteins that includes the cell division protein ZapA. The structure of ZapA has a core structure consisting of two layers alpha/beta, and has a long C-terminal helix that forms dimeric parallel and tetrameric antiparallel coiled coils.[1] ZapA interacts with FtsZ, where FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. ZapA drives the polymerisation and filament bundling of FtsZ, thereby contributing to the spatio-temporal tuning of the Z-ring.
References
- ^ Low HH, Moncrieffe MC, Löwe J (August 2004). "The crystal structure of ZapA and its modulation of FtsZ polymerisation". J. Mol. Biol. 341 (3): 839–52. doi:10.1016/j.jmb.2004.05.031. PMID 15288790.