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Structure paper

TitleAllosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.
Journal, issue, pagesMBio, Vol. 5, Page e02105-e02105, Year 2014
Publish dateJun 25, 2013 (structure data deposition date)
AuthorsTrajtenberg, F. / Albanesi, D. / Ruetalo, N. / Botti, H. / Mechaly, A.E. / Nieves, M. / Aguilar, P.S. / Cybulski, L. / Larrieux, N. / de Mendoza, D. / Buschiazzo, A.
External linksMBio / PubMed:25406381
MethodsX-ray diffraction
Resolution1.951 - 2.54 Å
Structure data

PDB-4ldz:
Crystal structure of the full-length response regulator DesR in the active state
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-4le0:
Crystal structure of the receiver domain of DesR in complex with beryllofluoride and magnesium
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

PDB-4le1:
Crystal structure of the receiver domain of DesR in the inactive state
Method: X-RAY DIFFRACTION / Resolution: 1.951 Å

PDB-4le2:
Crystal structure of the unphosphorylated receiver domain of DesR in the active state
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-PO4:
PHOSPHATE ION

ChemComp-K:
Unknown entry

Source
  • bacillus subtilis subsp. subtilis (bacteria)
KeywordsDNA BINDING PROTEIN / Response regulator / two-component system / transcription factor / receiver domain / DNA binding domain / phosphorylation / active state

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