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Structure paper

TitleA nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes.
Journal, issue, pagesNat. Chem. Biol., Vol. 16, Page 834-840, Year 2020
Publish dateJun 22, 2019 (structure data deposition date)
AuthorsTamman, H. / Van Nerom, K. / Takada, H. / Vandenberk, N. / Scholl, D. / Polikanov, Y. / Hofkens, J. / Talavera, A. / Hauryliuk, V. / Hendrix, J. / Garcia-Pino, A.
External linksNat. Chem. Biol. / PubMed:32393900
MethodsX-ray diffraction
Resolution2.75 - 2.96 Å
Structure data

PDB-6s2t:
Structure of the N-terminal catalytic region of T. thermophilus Rel bound to ppGpp
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-6s2u:
Structure of the catalytic domain of T. thermophilus Rel in complex with AMP and ppGpp
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-6s2v:
Structure of the N-terminal catalytic region of T. thermophilus Rel
Method: X-RAY DIFFRACTION / Resolution: 2.96 Å

Chemicals

ChemComp-G4P:
GUANOSINE-5',3'-TETRAPHOSPHATE

ChemComp-GOL:
GLYCEROL

ChemComp-MN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-GN3:
[[[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanylidene-1~{H}-purin-9-yl)-4-oxidanyl-2-[[oxidanyl(phosphonooxy)phosphoryl]oxymethyl]oxolan-3-yl]oxy-oxidanyl-phosphoryl]amino]phosphonic acid

ChemComp-TMO:
trimethylamine oxide

ChemComp-PO4:
PHOSPHATE ION

Source
  • thermus thermophilus (bacteria)
KeywordsTRANSFERASE / ppGpp hydrolase / ppGpp synthetase / Rel / ppGpp / translation / stringent response

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