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Structure paper

TitleWhat Glues a Homodimer Together: Systematic Analysis of the Stabilizing Effect of an Aromatic Hot Spot in the Protein-Protein Interface of the tRNA-Modifying Enzyme Tgt.
Journal, issue, pagesAcs Chem. Biol., Vol. 10, Page 1897-1907, Year 2015
Publish dateFeb 28, 2012 (structure data deposition date)
AuthorsJakobi, S. / Nguyen, P.T. / Debaene, F. / Cianferani, S. / Reuter, K. / Klebe, G.
External linksAcs Chem. Biol. / PubMed:25951081
MethodsX-ray diffraction
Resolution1.7 - 2.045 Å
Structure data

PDB-4dy1:
tRNA-guanine transglycosylase F92C C158S C281S mutant
Method: X-RAY DIFFRACTION / Resolution: 2.045 Å

PDB-4htb:
tRNA-guanine transglycosylase Y330C mutant in space group C2
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4l56:
tRNA guanine transglycosylase H333D mutant apo structure
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

Source
  • zymomonas mobilis (bacteria)
  • zymomonas mobilis subsp. mobilis (bacteria)
KeywordsTRANSFERASE / functional dimer / protein-protein interface / guanine exchange enzyme / zinc binding / guanine binding / tRNA binding / Protein-Protein-Interface / Dimer Interface / TGT / tRNA / guanine / GLYCOSYLTRANSFERASE / TRNA PROCESSING / METAL-BINDING / QUEUOSINE

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