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Structural and biochemical studies reveal a putative FtsZ recognition site on the Z-ring stabilizer ZapD
DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | 이형호 | - |
dc.contributor.author | 최화정 | - |
dc.date.accessioned | 2017-10-31T08:35:10Z | - |
dc.date.available | 2017-10-31T08:35:10Z | - |
dc.date.issued | 2017-08 | - |
dc.identifier.other | 000000145051 | - |
dc.identifier.uri | https://hdl.handle.net/10371/138110 | - |
dc.description | 학위논문 (석사)-- 서울대학교 대학원 자연과학대학 화학부, 2017. 8. 이형호. | - |
dc.description.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. | - |
dc.description.tableofcontents | Abstract i
Contents ii List of Figures iii List of Table iv І. Introduction 1 ІІ. Materials and Methods 10 1. Cloning and protein preparation 10 2. Crystallization, structure determination, and refinement 15 3. Size exclusion chromatography with multi-angle light scattering (SEC-MALS) 18 4. Bio-layer interferometry (BLI) measurement 18 III. Results and Discussion 20 1. Structure determination of EcZapD and StZapD 20 2. Overall structure of StZapD and its oligomeric state in solution 24 3. The binding activity of EcZapD to the C-terminal peptide of FtsZ 30 4. Putative FtsZ binding sites on EcZapD and modeled structure of EcZapD2-247-FtsZ367-383 complex 32 ІV. References 35 Abstract in Korean 40 | - |
dc.format | application/pdf | - |
dc.format.extent | 1813184 bytes | - |
dc.format.medium | application/pdf | - |
dc.language.iso | en | - |
dc.publisher | 서울대학교 대학원 | - |
dc.subject | cell division | - |
dc.subject | cytokinesis | - |
dc.subject | FtsZ | - |
dc.subject | ZapD | - |
dc.subject.ddc | 540 | - |
dc.title | Structural and biochemical studies reveal a putative FtsZ recognition site on the Z-ring stabilizer ZapD | - |
dc.type | Thesis | - |
dc.description.degree | Master | - |
dc.contributor.affiliation | 자연과학대학 화학부 | - |
dc.date.awarded | 2017-08 | - |
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