Structural highlights
Function
TPX_ECOLI Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space.[HAMAP-Rule:MF_00269]
Publication Abstract from PubMed
Thiol peroxidase (Tpx) is an atypical 2-Cys peroxiredoxin, which has been suggested to be important for cell survival and virulence in Gram-negative pathogens. The structure of a catalytically inactive version of this protein in an orthorhombic crystal form has been determined by molecular replacement. Structural alignments revealed that Tpx is conserved. Analysis of the crystal packing shows that the linker region of the affinity tag is important for formation of the crystal lattice.
The structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.,Beckham KS, Byron O, Roe AJ, Gabrielsen M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. Epub, 2012 Apr 20. PMID:22691780[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Beckham KS, Byron O, Roe AJ, Gabrielsen M. The structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. Epub, 2012 Apr 20. PMID:22691780 doi:10.1107/S1744309112011487
