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Structure paper

TitleBase Flipping by MTERF1 Can Accommodate Multiple Conformations and Occurs in a Stepwise Fashion.
Journal, issue, pagesJ. Mol. Biol., Vol. 428, Page 2542-2556, Year 2016
Publish dateJul 15, 2015 (structure data deposition date)
AuthorsByrnes, J. / Hauser, K. / Norona, L. / Mejia, E. / Simmerling, C. / Garcia-Diaz, M.
External linksJ. Mol. Biol. / PubMed:26523681
MethodsX-ray diffraction
Resolution2.48 - 2.65 Å
Structure data

PDB-5cky:
Crystal Structure of the MTERF1 R162A substitution bound to the termination sequence.
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

PDB-5co0:
Crystal Structure of the MTERF1 Y288A substitution bound to the termination sequence.
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-5crj:
Crystal Structure of the MTERF1 F322A substitution bound to the termination sequence.
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

PDB-5crk:
Crystal Structure of the MTERF1 F243A substitution bound to the termination sequence.
Method: X-RAY DIFFRACTION / Resolution: 2.48 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsTRANSCRIPTION/DNA / Protein-DNA / Transcription Factor / Mitochondria / Termination / TRANSCRIPTION-DNA complex

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