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Structure paper

TitleS-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.
Journal, issue, pagesJ. Mol. Biol., Vol. 428, Page 3737-3751, Year 2016
Publish dateDec 31, 2015 (structure data deposition date)
AuthorsEichmann, C. / Tzitzilonis, C. / Nakamura, T. / Kwiatkowski, W. / Maslennikov, I. / Choe, S. / Lipton, S.A. / Riek, R.
External linksJ. Mol. Biol. / PubMed:27473602
MethodsX-ray diffraction / NMR (solution)
Resolution1.5 - 1.66 Å
Structure data

PDB-5hbl:
Native rhodanese domain of YgaP prepared with 1mM DDT is S-nitrosylated
Method: X-RAY DIFFRACTION / Resolution: 1.617 Å

PDB-5hbo:
Native rhodanese domain of YgaP prepared without DDT is both S-nitrosylated and S-sulfhydrated
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-5hbp:
The crystal of rhodanese domain of YgaP treated with SNOC
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-5hbq:
C63D mutant of the rhodanese domain of YgaP
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-5lam:
Refined 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli
Method: SOLUTION NMR

PDB-5lao:
S-nitrosylated 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli
Method: SOLUTION NMR

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsTRANSFERASE / S-nitrosylation / S-sulfhydration. rhodanese / S-sulfhydration / rhodanese / MEMBRANE PROTEIN / Rhodanese domain of YgaP / PROTEIN / S-nitrosylated rhodanese domain of YgaP

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