Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase

European Journal of Biochemistry

Volumn 268, Issue 22, 2001, Pages 5842-5850

  Cort, John R ^a   Santhana Mariappan, S V ^b,c   Kim, Chang Yub ^b   Park, Min S ^b   Peat, Thomas S ^b,d   Waldo, Geoffrey S ^b   Terwilliger, Thomas C ^b   Kennedy, Michael A ^a  

^a PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF TEXAS AT SAN ANTONIO   (United States)

^d ELI LILLY AND COMPANY   (United States)

Author keywords

Dissimilatory sulfite reductase; DsrC; Helix turn helix; NMR; Pyrobaculum aerophilum

Indexed keywords

CYSTEINE; GLOBULAR PROTEIN; HELIX LOOP HELIX PROTEIN; PROTEIN; PROTEIN DSRC; REGULATOR PROTEIN; SULFITE REDUCTASE; UNCLASSIFIED DRUG;

ARCHAEBACTERIUM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISULFIDE BOND; DNA BINDING; ENZYME SUBUNIT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; PYROBACULUM AEROPHILUM; REDUCTION; SAMPLE; THERMOPHILIC BACTERIUM;

AMINO ACID SEQUENCE; BASE SEQUENCE; DNA PRIMERS; HYDROGENSULFITE REDUCTASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; THERMOPROTEACEAE;

EID: 0035162654     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02529.x     Document Type: Article

References (47)

1. Dissimilatory reduction of sulfur compounds
2. Dissimilatory sulphite reductase from Archaeoglobus fulgidus: Physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes
3. A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum
4. Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
5. Siroheme sulfite reductase from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties
6. Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies
7. The relationship between structure and function for the sulfite reductases
8. The third subunit of desulfoviridin-type dissimilatory sulfite reductases
9. The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirehemes and S=9/2 iron-sulfur clusters
10. Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough)
11. Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory sulfite reductase and of the alpha- and beta-subunit genes is not coordinately regulated
12. Overexpression, purification and immunodetection of DsrD from Desulfovibrio vulgaris Hildenborough
13. Dissimilatory sulfite reductase (desulfoviridin) of the taurine-degrading, non-sulfate reducing bacterium Bilophila wadsworthia RZATAU contains a fused DsrB-DsrD subunit
14. The siroheme-sulfite reductase-type protein from Pyrobaculum islandicum
15. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
16. Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum
17. Pyrobaculum gen. nov., a new genus of neutrophilic, rod-shaped archaebacteria from continental solfataras growing optimally at 100°C
18. A fosmid-based genomic map and identification of 474 genes of the hyperthermophilic archaeon Pyrobaculum aerophilum
19. Selecting targets for structural genomics of Pyrobaculum aerophilum: Validating automated fold assignment methods by using binary hypothesis testing
20. Rapid protein-folding assay using green fluorescent protein
21. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
22. 15N-enriched proteins
23. α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
24. 15N-labeled proteins
25. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
26. 2O
27. Accurate measurements of proton scalar coupling constants using carbon-13 isotropic mixing spectroscopy
28. 13C magnetization
29. A general method for assigning NMR spectra of denatured proteins using 3D HC (CO) NH-TOCSY triple resonance experiments
30. 2O
31. 13C-separated HMQC-NOESY-HMQC spectra using pulsed field gradients
32. 13C labeling
33. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
34. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
35. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
36. Protein structure comparison by alignment of distance matrices
37. Mapping the protein universe
38. 13C NMR chemical shifts can predict disulfide bond formation
39. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
40. Sulfite reductase structure at 1.6 Å: Evolution and catalysis for reduction of inorganic ions
41. Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: Structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products
42. Desulfoviridin, the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex): New structural and functional aspects of the membranous enzyme