Naslov
Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium

Autori
Kekez, Ivana

Vrsta, podvrsta i kategorija rada
Ocjenski radovi, doktorska disertacija

Fakultet
Prirodoslovno-matematički fakultet

Mjesto
Zagreb

Datum
04.07

Godina
2016

Stranica
115+xxxii

Mentor
Matković-Čalogović, Dubravka ; Zanotti, Giuseppe

Ključne riječi
CrdA ; FlgD ; HP1026 ; H. pylori ; structural characterization

Sažetak
Within this thesis several proteins from H. pylori, important for survival of the bacterium, were structurally characterized (HpFlgD, CrdA, HP1026). Crystal structure of the truncated form of the HpFlgD protein revealed that spatial orientation of the two domains differs from that of the homologous FlgD family members. This fact together with the observation that truncated HpFlgD assembles into tetramers, both in the solution and in the crystal form, strongly suggests that significant differences exist in the molecular organization of the flagella in different bacterial species. It was shown that incubation of the putative copper binding CrdA protein with Cu2+ ions favours formation of monomeric species in solution and that CrdA binds Cu2+ with very low affinity which is a property of copper trafficking proteins. Functional assays of the HP1026 protein demonstrated for the first time its ATPase activity. While proteins that belong to the class of AAA+ proteins usually form hexamers, HP1026 was found to form dimers.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA