Publications
Detailed Information
Structural and biochemical studies reveal a putative FtsZ recognition site on the Z-ring stabilizer ZapD
Cited 0 time in
Web of Science
Cited 0 time in Scopus
- Authors
- Advisor
- 이형호
- Major
- 자연과학대학 화학부
- Issue Date
- 2017-08
- Publisher
- 서울대학교 대학원
- Keywords
- cell division ; cytokinesis ; FtsZ ; ZapD
- Description
- 학위논문 (석사)-- 서울대학교 대학원 자연과학대학 화학부, 2017. 8. 이형호.
- Abstract
- FtsZ, a tubulin homologue, is an essential protein of the Z-ring assembly in
bacterial cell division. It consists of two domains, the N-terminal and C-terminal
core domains, and has a conserved C-terminal tail region. Lateral interactions
between FtsZ protofilaments and several Z-ring associated proteins (Zaps) are
necessary for modulating Z-ring formation. ZapD, one of the positive regulators
of Z-ring assembly, directly binds to the C-terminal tail of FtsZ and promotes
stable Z-ring formation during cytokinesis. To gain structural and functional
insights into how ZapD interacts with the C-terminal tail of FtsZ, we solved two
crystal structures of ZapD proteins from Salmonella typhimurium (StZapD) and
Escherichia coli (EcZapD) at a 2.6 and 3.1 Å resolution, respectively. Several
conserved residues are clustered on the concave sides of the StZapD and EcZapD
dimers, the suggested FtsZ binding site. Modeled structures of EcZapD-EcFtsZ
and subsequent binding studies using bio-layer interferometry also identified the
EcFtsZ binding site on EcZapD. The structural insights and the results of bio
layer interferometry assays suggest that the two FtsZ binding sites of ZapD dimer
might be responsible for the binding of ZapD dimer to two protofilaments to hold
them together.
- Language
- English
- Files in This Item:
- Appears in Collections:
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.