Solution Structure of Pyrobaculum aerophilum DsrC, an Archaeal Homologue of the Gamma Subunit of Dissimilatory Sulfite Reductase
The solution structure of DsrC, an archaeal homologue of the g subunit of dissimilatory sulfite reductase has been determined by NMR spectroscopy. This 12.7 kDa protein from the hyperthermophilic archaeon Pyrobaculum aerophilum adopts a novel fold consisting of an orthogonal helical bundle with a b-hairpin along one side. A portion of the structure resembles the helix-turn-helix DNA-binding motif common in transcriptional regulator proteins. The protein contains two disulfide bonds but remains folded in the presence of DTT. DsrC proteins from organisms other than Pyrobaculum species do not contain these disulfide bonds. A conserved cysteine next to the C-terminus, which is not involved in the disulfide bonds, is not part of the globular structure of the protein and is located on an unstructured 7-residue C-terminal arm that extends away from the center of the protein.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Organization:
- US Department of Energy (US)
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 15011346
- Report Number(s):
- PNWD-SA-5402; 2053; TRN: US200506%%270
- Journal Information:
- European Journal of Biochemistry/FEBS, Vol. 268, Issue 22; Other Information: PBD: 29 Nov 2001
- Country of Publication:
- United States
- Language:
- English
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