<> "The repository administrator has not yet configured an RDF license."^^ . <> . . "On the Structure and Function of the COPI coat protein complex Coatomer"^^ . "In eukaryotes newly synthesized proteins and membranes in the early secretory pathway are transported by COPII and COPI vesicles. The key componets for the formation of COPI vesicles are the small GTPase Arf1 and the Coatomer complex. Coatomer is recruited to the donor mebrane by GTP-loaded Arf. On the membrane, coatomer polymerizes and deforms the membrane into a coated bud, which can then pinch of to form a free COPI vesicle. Prior to fusion of a vesicle with its target membrane, the coat is removed from the carrier by hydrolysis of GTP in Arf1.\r\nIn this work I investigated the structure of the coatomer complex and its interaction with the small GTPase Arf1.\r\nTo this end I decided to use coatomer and Arf derieved from the thermophilic ascomycete Chaetomium thermophilum, as proteins from this organism have proven more suitable for structural investigations as proteins from mesophilic organisms. We were able to produce coatomer from Chaetomium thermophilum and showed that it produces COPI vesicles. Also we prepared coatomer variants lacking the e-COP subunit and the C-terminal m-homology domain of d-COP. e-COP and the m-homolgy domain of d-COP have been implicated in forming contacts between coatomer triads on COPI-vesicles to stabilize the coat on the membrane. Surprisingly both coatomer variants retained the ability to produce vesicles.\r\nThe structure of the coatomer complex was only partially solved at the atomic level. In this work we were able to solve the structure of a bd-subcomplex of coatomer. The structural information of this complex closes the largest gap in our knowledge of atomic coatomer structure. The structure shows a close homology to gz-COP. The N-terminal part of g-COP and b-COP both form curved a-solenoid folds, whereas z-COP and the N-terminal part of d-COP form longin-like folds. Our structure reveals that an extended linker region of d-COP passes below the a-solenoid of b-COP. The passage of the linker is close to an assumed binding site of the small GTPase Arf1 on b-COP, implicating a potential function of the linker in Arf-binding.\r\nTwo major binding sites on coatomer for Arf are implicated in the initial recruitment of the coat complex. One site is situated on g-COP and the other on b-COP. In addition, the d-COP subunit had been reported to bind Arf. We show here that the affinity of bd-subcomplexes to bind Arf is increased by incorporation of the first two a-helices of the linker region of d-COP. This data revealed that b-COP and d-COP bind to the same Arf molecule."^^ . "2016" . . . . . . . "Patrick"^^ . "Aderhold"^^ . "Patrick Aderhold"^^ . . . . . . "On the Structure and Function of the COPI coat protein complex Coatomer (PDF)"^^ . . . "Dissertation_Patrick Aderhold.pdf"^^ . . . "On the Structure and Function of the COPI coat protein complex Coatomer (Other)"^^ . . . . . . "lightbox.jpg"^^ . . . "On the Structure and Function of the COPI coat protein complex Coatomer (Other)"^^ . . . . . . "preview.jpg"^^ . . . "On the Structure and Function of the COPI coat protein complex Coatomer (Other)"^^ . . . . . . "medium.jpg"^^ . . . "On the Structure and Function of the COPI coat protein complex Coatomer (Other)"^^ . . . . . . "small.jpg"^^ . . . "On the Structure and Function of the COPI coat protein complex Coatomer (Other)"^^ . . . . . . "indexcodes.txt"^^ . . "HTML Summary of #22038 \n\nOn the Structure and Function of the COPI coat protein complex Coatomer\n\n" . "text/html" . . . "570 Biowissenschaften, Biologie"@de . "570 Life sciences"@en . .