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Structure paper

TitleMajor Reorientation of tRNA Substrates Defines Specificity of Dihydrouridine Synthases.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 112, Page 6033-, Year 2015
Publish dateMar 16, 2013 (structure data deposition date)
AuthorsByrne, R.T. / Jenkins, H.T. / Peters, D.T. / Whelan, F. / Stowell, J. / Aziz, N. / Kasatsky, P. / Rodnina, M.V. / Koonin, E.V. / Konevega, A.L. / Antson, A.A.
External linksProc. Natl. Acad. Sci. USA / PubMed:25902496
MethodsX-ray diffraction
Resolution1.65 - 2.6 Å
Structure data

PDB-4bf9:
Crystal structure of E. coli dihydrouridine synthase C (DusC) (selenomethionine derivative)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4bfa:
Crystal structure of E. coli dihydrouridine synthase C (DusC)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4yco:
E. coli dihydrouridine synthase C (DusC) in complex with tRNAPhe
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4ycp:
E. coli dihydrouridine synthase C (DusC) in complex with tRNATrp
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-NO3:
NITRATE ION

ChemComp-MG:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli (strain k12) (bacteria)
KeywordsOXIDOREDUCTASE / TRNA MODIFICATION / Oxidoreductase/RNA / oxidoreductase-RNA complex

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