Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR042233
ZapA is a cell division protein which interacts with FtsZ. 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. The interaction of FtsZ with ZapA drives its polymerisation and promotes FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring
[1].
The structure of ZapA is organised into two distinct domains, with the first 49 residues forming a globular domain comprised of a two stranded antiparallel β-sheet and an α-helix, whereas the C-terminal half of the protein (residues 50-102) forms a single, 14-turn α-helix. The ZapA protomer forms a pseudosymmetric tetramer.
This superfamily represents a domain found at the N terminus of the cell division protein ZapA. Its structure is composed of an α-helix which plays a role in mediating ZapA-FtsZ interactions to facilitate FtsZ filament bundling and Z-ring stability in dividing bacterial cells.
References Imported from IPR042233
1.The crystal structure of ZapA and its modulation of FtsZ polymerisation. Low HH, Moncrieffe MC, Lowe J. J. Mol. Biol. 341, 839-52, (2004). View articlePMID: 15288790