Significant changes between the X-ray structure and NMR structure of delta subunit of RNA polymerase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00057460" target="_blank" >RIV/00216224:14740/12:00057460 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
čeština
Original language name
Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase
Original language description
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.
Czech name
Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase
Czech description
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.
Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GD301%2F09%2FH004" target="_blank" >GD301/09/H004: Molecular and structural biology of selected antitumor drugs. From mechanistic studies to chemotherapy of tumors</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů