dissimilatory sulfite reductase

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Word Map on EC


a [DsrC protein]-S-sulfanyl-L-cysteine
+ 2 acceptor + 3 H2O =
a [DsrC protein]-dithiol
+ 2 reduced acceptor + 2 H+


dSiR, DsrA, DsrAB, DsrC, DsvA, DsvB, hydrogen-sulfide:(acceptor) oxidoreductase, octahaemcytochrome c MccA, PAE2566, SiRA, siroheme sulfite reductase, sulfite reductase


     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.99 With unknown physiological acceptors
       dissimilatory sulfite reductase


Crystallization on EC - dissimilatory sulfite reductase

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modeling of three dimensional strucuture of the alpha2beta2 hetero-tetrameric protein complex
crystal structure at 2 A resolution and comparison with that of the phylogenetically related assimilatory sulfite reductase aSir. Dissimilatory sulfite reductase dSir is organized as a heterotetrameric complex composed of two catalytically independent alphabeta heterodimers. aSir is a monomeric protein built of two fused modules. aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue
structure of gamma-subunit DsrC, native protein to 1.12 A, and in complex with tert-butyl hydroperoxide to 2.1 A resolution. The highly conserved C-terminal arm adopts a well-defined conformation. The disulfide bond between Cys77 and Cys85 connects helices alpha3 and alpha4 and presumably plays a structural role to stabilize the protein
to 1.37 A resolution, space group P41212, with unit-cell parameters a = b = 163.26, c = 435.32 A. The crystal contains three alpha2beta2gamma2 units per asymmetric unit,
to 2.8 A resolution, space group P21 with unit-cell parameters a = 122.7, b = 119.4 and c = 146.7 A and b =110.0 degrees
solution structure of subunit DsrC adopts a fold consisting of an orthogonal helical bundle with a beta-hairpin along one side. The protein contains two disulfide bonds but remains folded following reduction of the disulfides. A conserved cysteine next to the C-terminus is located on a seven-residue C-terminal arm that is not part of the globular protein
purified enzyme, X-ray diffraction structure determination and analysis at 2.2 A resolution, single-wavelength anomalous dispersion