Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium (CROSBI ID 405353)
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Podaci o odgovornosti
Kekez, Ivana
Matković-Čalogović, Dubravka ; Zanotti, Giuseppe
engleski
Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium
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.
CrdA ; FlgD ; HP1026 ; H. pylori ; structural characterization
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Podaci o izdanju
115+xxxii
04.07.2016.
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Podaci o ustanovi koja je dodijelila akademski stupanj
Prirodoslovno-matematički fakultet, Zagreb
Zagreb