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  X-ray structure of the γ-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms

Mander, G. J., Weiss, M. S., Hedderich, R., Kahnt, J., Ermler, U., & Warkentin, E. (2005). X-ray structure of the γ-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms. FEBS Letters, 579(21), 4600-4604. doi:10.1016/j.febslet.2005.07.029.

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 Creators:
Mander, Gerd J.1, Author
Weiss, Manfred S.2, Author
Hedderich, Rainer1, Author
Kahnt, Jörg1, Author
Ermler, Ulrich3, Author           
Warkentin, Eberhard3, Author           
Affiliations:
1Max-Planck-Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany, ou_persistent22              
2EMBL Hamburg Outstation, c/o DESY, 22603 Hamburg, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Sulfite reductase; Disulfide bond; C-terminal arm; Conformational flexibility; Archaeoglobus fulgidus
 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 DsrCnat and DsrCox 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.

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Language(s): eng - English
 Dates: 2005-07-042005-05-272005-07-042005-08-012005-08-29
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.febslet.2005.07.029
PMID: 16098517
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 579 (21) Sequence Number: - Start / End Page: 4600 - 4604 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501