2A5W

Crystal structure of the oxidized gamma-subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus

Summary for 2A5W

• Entry DOI: 10.2210/pdb2a5w/pdb
• Related: 1SAU
• Descriptor: sulfite reductase, desulfoviridin-type subunit gamma (dsvC), SULFATE ION (3 entities in total)
• Functional Keywords: orthogonal helix bundle, oxidoreductase
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 3
• Total formula weight: 40880.23

Authors

Mander, G.J.,Weiss, M.S.,Hedderich, R.,Kahnt, J.,Ermler, U.,Warkentin, E. (deposition date: 2005-07-01, release date: 2005-09-06, Last modification date: 2024-11-20)

Primary citation

Mander, G.J.,Weiss, M.S.,Hedderich, R.,Kahnt, J.,Ermler, U.,Warkentin, E.
X-ray structure of the gamma-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms.
Febs Lett., 579:4600-4604, 2005

PubMed Abstract: The X-ray structure of the gamma-subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus was determined at 1.12 and 2.1A 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.

PubMed: 16098517
DOI: 10.1016/j.febslet.2005.07.029

Experimental method

X-RAY DIFFRACTION (2.1 Å)