prikaz prve stranice dokumenta Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium
  Download
PDF 5.83 MB
doctoral thesis
Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium
Zagreb: University of Zagreb, Faculty of Science, 2016. urn:nbn:hr:217:633407
Kekez, Ivana
University of Zagreb
Faculty of Science
Department of Chemistry

Cite this document

Kekez, I. (2016). Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium (Doctoral thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:633407

Kekez, Ivana. "Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium." Doctoral thesis, University of Zagreb, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:217:633407

Kekez, Ivana. "Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium." Doctoral thesis, University of Zagreb, Faculty of Science, 2016. https://urn.nsk.hr/urn:nbn:hr:217:633407

Kekez, I. (2016). 'Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium', Doctoral thesis, University of Zagreb, Faculty of Science, accessed 20 April 2024, https://urn.nsk.hr/urn:nbn:hr:217:633407

Kekez I. Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium [Doctoral thesis]. Zagreb: University of Zagreb, Faculty of Science; 2016 [cited 2024 April 20] Available at: https://urn.nsk.hr/urn:nbn:hr:217:633407

I. Kekez, "Structural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium", Doctoral thesis, University of Zagreb, Faculty of Science, Zagreb, 2016. Available at: https://urn.nsk.hr/urn:nbn:hr:217:633407

Please login to the repository to save this object to your list.
Metadata
TitleStructural characterization of Heliobacter plyori proteinsrequired for survival of the bacterium
Title (croatian)Strukturna karakterizacija proteina bakterije Helicobacter pylori važnih za njezino preživljavanje
AuthorIvana Kekez
MentorDubravka Matković-Čalogović (mentor)
MentorGiuseppe Zanotti https://orcid.org/0000-0002-0945-6501 (mentor)
Committee memberJasmina Rokov Plavec (predsjednik povjerenstva)
Committee memberDubravka Matković-Čalogović (član povjerenstva)
Committee memberMarija Luić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2016-07-04, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Inorganic Chemistry
Universal decimal classification
(UDC)		54 - Chemistry. Crystallography. Mineralogy
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.
Abstract (croatian)
U sklopu ove disertacije strukturno su okarakterizirani proteini iz bakterije H. pylori koji su važni za njezino preživljavanje (HpFlgD, CrdA, HP1026). Riješena kristalna struktura skraćenog proteina HpFlgD ukazala je na drugačiju međusobnu orijentaciju dviju domena nego što je nađeno u ostalim homolozima proteina FlgD. Također je pokazano da je skraćeni HpFlgD i u otopini i kristalu prisutan kao tetramer što ukazuje na značajnu razliku u molekularnoj organizaciji biča u različitih bakterijskih vrsta. Uočeno je da dodatak iona Cu2+ u otopinu CrdA, proteina koji pretpostavljeno veže bakrove ione, potiče stvaranje monomernih vrsta u otopini te da CrdA veže ione Cu2+ sa slabim afinitetom što je karakteristika proteina koji prenose bakrove ione. Funkcionalna karakterizacija proteina HP1026 je po prvi put demonstrirala da HP1026 obavlja ATPaznu aktivnost. Iako se proteni koji spadaju u skupinu AAA+ proteina najčešće udružuju kao heksameri, za HP1026 je pokazano da u otopini stvara dimerne vrste.
Keywords
Keywords (croatian)
Languageenglish
URN:NBNurn:nbn:hr:217:633407
Study programmeTitle: Doctoral study in chemistry
Study programme type: university
Study level: postgraduate
Academic / professional title: doktor/doktorica znanosti, područje prirodnih znanosti, polje kemija (doktor/doktorica znanosti, područje prirodnih znanosti, polje kemija)
Type of resourceText
Extent147 str. ; 30 cm
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
RepositoryRepository of the Faculty of Science
Created on2017-02-03 10:22:42

(©) Nacionalna i sveučilišna knjižnica u Zagrebu 2015. Sva prava pridržana. | Hrvatske bratske zajednice 4 p.p. 550, 10000 Zagreb, Hrvatska Tel. ++ 385 1 616-4040
OIB: 84838770814 | IBAN: HR66 2340 0091 1000 1008 1, Porezni broj (PDV identifikacijski broj) - VAT Number: HR84838770814
Prijava u repozitorij