4AF2

C61S mutant of thiol peroxidase form E. coli.

Summary for 4AF2

Entry DOI	10.2210/pdb4af2/pdb
Descriptor	THIOL PEROXIDASE (2 entities in total)
Functional Keywords	oxidoreductase, inactive mutant, peroxiredoxin
Biological source	ESCHERICHIA COLI
Cellular location	Periplasm (By similarity): P0A864
Total number of polymer chains	1
Total formula weight	21622.41
Authors	Beckham, K.S.H.,Roe, A.J.,Byron, O.,Gabrielsen, M. (deposition date: 2012-01-16, release date: 2012-05-02, Last modification date: 2023-12-20)
Primary citation	Beckham, K.S.H.,Byron, O.,Roe, A.J.,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, 68:522-, 2012 Cited by PubMed Abstract: 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. PubMed: 22691780 DOI: 10.1107/S1744309112011487 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.97 Å)

Structure validation