Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase

Varování

Publikace nespadá pod Filozofickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.

Autoři	DEMO Gabriel PAPOUŠKOVÁ Veronika ŠANDEROVÁ Hana ŽÍDEK Lukáš WIMMEROVÁ Michaela
Rok publikování	2012
Druh	Konferenční abstrakty
Fakulta / Pracoviště MU	Středoevropský technologický institut
Citace
Popis	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.
Související projekty:	Molekulární a strukturní biologie vybraných cytostatik. Od mechanických studií k chemoterapii rakoviny