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ZapA family

From Wikipedia, the free encyclopedia
ZapA
The crystal structure of the bacterial cell division protein ZapA
Identifiers
SymbolZapA
PfamPF05164
InterProIPR007838
SCOP21t3u / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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  1. ^ 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.
This article incorporates text from the public domain Pfam and InterPro: IPR007838