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X‐ray structure of the γ‐subunit of a dissimilatory sulfite reductase: Fixed and flexible C‐terminal arms
Author(s) -
Mander Gerd J.,
Weiss Manfred S.,
Hedderich Reiner,
Kahnt Jörg,
Ermler Ulrich,
Warkentin Eberhard
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.07.029
Subject(s) - sulfite reductase , chemistry , sulfite , protein subunit , stereochemistry , biochemistry , reductase , enzyme , gene
The X‐ray structure of the γ‐subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus was determined at 1.12 and 2.1 Å resolution, in the two crystal forms named DsrC nat and DsrC ox the latter being cocrystallized with the oxidizing agent tert ‐butyl hydroperoxide. The fold corresponds to that of the homologous protein from Pyrobaculum aerophilum but is significantly more compact. The most interesting, highly conserved C‐terminal arm adopts a well‐defined conformation in A. fulgidus DsrC in contrast to the completely disordered conformation in P. aerophilum DsrC. The functional relevance of both conformations and of a potentially redox‐active disulfide bond between the strictly invariant Cys103 and Cys114 are discussed.