DEMO, Gabriel, Veronika PAPOUŠKOVÁ, Hana ŠANDEROVÁ, Lukáš ŽÍDEK and Michaela WIMMEROVÁ. Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase (Significant changes between the X-ray structure and NMR structure of delta subunit of RNA polymerase). In Struktura 2012, Cesko-slovenska krystalograficka spolecnost. 2012. ISSN 1211-5894.
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Basic information
Original name Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase
Name in Czech Podstatni zmeny mezi krystalografickou a NMR strukturou delta podjednotky RNA polymerazy
Name (in English) Significant changes between the X-ray structure and NMR structure of delta subunit of RNA polymerase
Authors DEMO, Gabriel (703 Slovakia, belonging to the institution), Veronika PAPOUŠKOVÁ (203 Czech Republic, belonging to the institution), Hana ŠANDEROVÁ (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution).
Edition Struktura 2012, Cesko-slovenska krystalograficka spolecnost, 2012.
Other information
Original language Czech
Type of outcome Conference abstract
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14740/12:00057460
Organization unit Central European Institute of Technology
ISSN 1211-5894
Keywords (in Czech) delta podjednotka NMR krystalograficka struktura porovnani
Keywords in English delta subunit comparism NMR Xray structure
Changed by Changed by: Mgr. Gabriel Demo, Ph.D., učo 150765. Changed: 29/6/2012 10:22.
Abstract
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.
Abstract (in English)
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.
Links
GD301/09/H004, research and development projectName: Molekulární a strukturní biologie vybraných cytostatik. Od mechanistických studií k chemoterapii rakoviny
Investor: Czech Science Foundation
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