Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium

Kekez, Ivana (2016) Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium. Doctoral thesis, Faculty of Science > Department of Chemistry.

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Abstract

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.

Item Type: Thesis (Doctoral thesis)
Keywords: CrdA, FlgD, HP1026, H. pylori, structural characterization
Supervisor: Matković-Čalogović, Dubravka and Zanotti, Giuseppe
Date: 2016
Number of Pages: 147
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Faculty of Science > Department of Chemistry
Depositing User: Branka Maravic
Date Deposited: 14 Jul 2016 12:53
Last Modified: 14 Jul 2016 12:53
URI: http://digre.pmf.unizg.hr/id/eprint/4977

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