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Structure paper

TitleActivation of the LicT Transcriptional Antiterminator Involves a Domain Swing/Lock Mechanism Provoking Massive Structural Changes
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 14780-14789, Year 2005
Publish dateJun 10, 2004 (structure data deposition date)
AuthorsGraille, M. / Zhou, C.-Z. / Receveur-Brechot, V. / Collinet, B. / Declerck, N. / van Tilbeurgh, H.
External linksJ. Biol. Chem. / PubMed:15699035
MethodsX-ray diffraction
Resolution1.95 Å
Structure data

PDB-1tlv:
Structure of the native and inactive LicT PRD from B. subtilis
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bacillus subtilis (bacteria)
KeywordsTRANSCRIPTION / transcriptional antitermination / conformational change / LicT / histidine phosphorylation / activation mechanism / HPr / dimer structure / phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) / PTS regulation domains (PRD)

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