2012
Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase
DEMO, Gabriel; Veronika PAPOUŠKOVÁ; Hana ŠANDEROVÁ; Lukáš ŽÍDEK; Michaela WIMMEROVÁ et al.Základní údaje
Originální název
Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase
Název česky
Podstatni zmeny mezi krystalografickou a NMR strukturou delta podjednotky RNA polymerazy
Název anglicky
Significant changes between the X-ray structure and NMR structure of delta subunit of RNA polymerase
Autoři
Vydání
Struktura 2012, Cesko-slovenska krystalograficka spolecnost, 2012
Další údaje
Jazyk
čeština
Typ výsledku
Konferenční abstrakt
Obor
10600 1.6 Biological sciences
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14740/12:00057460
Organizační jednotka
Středoevropský technologický institut
ISSN
Klíčová slova česky
delta podjednotka NMR krystalograficka struktura porovnani
Klíčová slova anglicky
delta subunit comparism NMR Xray structure
Změněno: 29. 6. 2012 10:22, Mgr. Gabriel Demo, Ph.D.
V originále
RNA polymerase is an essential enzyme. RNAP from gram negative bacteria contain two additional subunits. The delta subunit is 173 aminoacids long and comes from Bacillus subtilis. The N terminal domain displays an ordered structure and the C terminal domain appears to be flexible and unstructured. The N terminal domain was solved either with NMR and Xray. The Xray structure showed completely different behaviour in the region corresponding to beta sheets present in NMR structure. In the Xray structure were found nickel ions which may have a significant effect on the folding of the protein. This is a strong proof that some of the proteins can be differently structured in the solution as in the crystalline phase.
Anglicky
RNA polymerase is an essential enzyme. RNAP from gram negative bacteria contain two additional subunits. The delta subunit is 173 aminoacids long and comes from Bacillus subtilis. The N terminal domain displays an ordered structure and the C terminal domain appears to be flexible and unstructured. The N terminal domain was solved either with NMR and Xray. The Xray structure showed completely different behaviour in the region corresponding to beta sheets present in NMR structure. In the Xray structure were found nickel ions which may have a significant effect on the folding of the protein. This is a strong proof that some of the proteins can be differently structured in the solution as in the crystalline phase.
Návaznosti
| GD301/09/H004, projekt VaV |
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