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Structure paper

TitleAnalysis of the Link between Enzymatic Activity and Oligomeric State in AhpC, a Bacterial Peroxiredoxin.
Journal, issue, pagesBiochemistry, Vol. 44, Page 10583-10592, Year 2005
Publish dateDec 28, 2004 (structure data deposition date)
AuthorsParsonage, D. / Youngblood, D.S. / Sarma, G.N. / Wood, Z.A. / Karplus, P.A. / Poole, L.B.
External linksBiochemistry / PubMed:16060667
MethodsX-ray diffraction
Resolution2.3 - 2.6 Å
Structure data

PDB-1yep:
Structural and biochemical analysis of the link between enzymatic activity and olgomerization in AhpC, a bacterial peroxiredoxin.
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1yex:
Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1yf0:
Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin.
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1yf1:
Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin.
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • salmonella typhimurium (bacteria)
KeywordsOXIDOREDUCTASE / AHPC / Peroxiredoxin / peroxidase / Alkyl hydroperoxide reductase subunit C

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