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Structure paper

TitleStructure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.
Journal, issue, pagesRNA, Vol. 24, Page 926-938, Year 2018
Publish dateDec 12, 2017 (structure data deposition date)
AuthorsPichard-Kostuch, A. / Zhang, W. / Liger, D. / Daugeron, M.C. / Letoquart, J. / Li de la Sierra-Gallay, I. / Forterre, P. / Collinet, B. / van Tilbeurgh, H. / Basta, T.
External linksRNA / PubMed:29650678
MethodsX-ray diffraction
Resolution2.62 - 2.86 Å
Structure data

PDB-6f87:
Crystal structure of P. abyssi Sua5 complexed with L-threonine and PPi
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

PDB-6f89:
Structure of H234A/Y235A P.abyssi Sua5
Method: X-RAY DIFFRACTION / Resolution: 2.81 Å

PDB-6f8y:
Crystal structure of P. abyssi Sua5 complexed with L-threonine
Method: X-RAY DIFFRACTION / Resolution: 2.86 Å

Chemicals

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-THR:
THREONINE

ChemComp-HOH:
WATER

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

Source
  • pyrococcus abyssi (strain ge5 / orsay) (archaea)
KeywordsTRANSFERASE / Nucleotidyltransferase / tRNA modification / threonylcarbamoylation

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