1996
DOI: 10.1002/pro.5560050713
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Abstract: Crystals of the tetraheme cytochrome c3 from sulfate-reducing bacteria Desulfovibrio gigas (Dg) (MW 13 kDa, 11 1 residues, four heme groups) were obtained and X-ray diffraction data collected to 1.8 A resolution. The structure was solved by the method of molecular replacement and the resulting model refined to a conventional R-factor of 14.9%. The three-dimensional structure shows many similarities to other known crystal structures of tetraheme c3 cytochromes, but it also shows some remarkable differences. In … Show more

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Cited by 73 publications
(69 citation statements)
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References 31 publications
(24 reference statements)
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“…A comparison with those of 4-heme and 8-heme cytochromes c 3 from Desulfovibrio, as they result from the analysis of the crystal structures, is also reported. High-resolution (1.7Ϫ2.2 Å ) X-ray structures are available for the tetraheme cytochromes from D. desulfuricans (ATCC 27774 [16] and Norway strain [21]), Desulfovibrio gigas [20], Desulfovibrio vulgaris (Hildenborough [15] and Miyazaki [17]), and for an octaheme cytochrome from D. desulfuricans [19]. The latter protein is a dimeric protein, each subunit containing four hemes.…”
Section: Resultsmentioning
confidence: 99%
“…A comparison with those of 4-heme and 8-heme cytochromes c 3 from Desulfovibrio, as they result from the analysis of the crystal structures, is also reported. High-resolution (1.7Ϫ2.2 Å ) X-ray structures are available for the tetraheme cytochromes from D. desulfuricans (ATCC 27774 [16] and Norway strain [21]), Desulfovibrio gigas [20], Desulfovibrio vulgaris (Hildenborough [15] and Miyazaki [17]), and for an octaheme cytochrome from D. desulfuricans [19]. The latter protein is a dimeric protein, each subunit containing four hemes.…”
Section: Resultsmentioning
confidence: 99%
“…This is still the case for the tetrahaem cytochromes c 3 from Desulfovibrio spp., even though considerable progress has been made in rationalising their thermodynamic properties (Santos et al, 1984;Coletta et al, 1991;Turner et al, 1994Turner et al, , 1996Park et al, 1996;Louro et al, 1996;Salgueiro et al, 1997) and high-resolution X-ray structures are available for several cytochromes c 3 in the oxidised form (Higuchi et al, 1984;Czjzek et al, 1994;Matias et al, 1996;Simo Ä es et al, 1998). Tetrahaem cytochrome c 3 from Desulfovibrio vulgaris (Hildenborough: DvHc 3 ) is a small (14 kDa; 107 amino acid residues) soluble protein whose crystal structure in the oxidised state has been determined by X-ray diffraction (Matias et al, 1993;Simo Ä es et al, 1998).…”
Section: Introductionmentioning
confidence: 99%
“…Although the molecular basis for the ®ne regulation of several types of cooperativity mechanisms has been successfully established (Perutz, 1990), including redox-linked regulation in enzyme catalysis (Williams et al, 1997;Fu È lo È p et al, 1995;Fukuyama et al, 1995;Chen et al, 1994), no unequivocal structural basis for the cooperativity involved in electronic to protonic energy transduction has been established. This is still the case for the tetrahaem cytochromes c 3 from Desulfovibrio spp., even though considerable progress has been made in rationalising their thermodynamic properties (Santos et al, 1984;Coletta et al, 1991;Turner et al, 1994Turner et al, , 1996Park et al, 1996;Louro et al, 1996;Salgueiro et al, 1997) and high-resolution X-ray structures are available for several cytochromes c 3 in the oxidised form (Higuchi et al, 1984;Czjzek et al, 1994;Matias et al, 1996;Simo Ä es et al, 1998).…”
Section: Introductionmentioning
confidence: 99%
“…This ligation is unlike typical class I cytochromes where the peptide carbonyl of a conserved Pro residue (Pro 30 in mitochondrial cytochrome c) provides the hydrogen bond partner for the histidine. Water as a hydrogen bonding partner to the histidine N1 has been reported for some of the heme groups in tetraheme cytochromes (28,29), and it is the hydrogen bonding partner in nitrophorin (5) and FixL (3). The imidazole aromatic plane forms a dihedral angle of 28°with the N2-Fe-N4 line in SHP, which is far from the ideal value of 45°.…”
mentioning
confidence: 98%
“…The imidazole group is wedged in a hydrophobic pocket lining the proximal heme face. This pocket is formed by the side chains of residues Phe 29 . The imidazole moiety is restrained through a water-mediated hydrogen bond to the backbone oxygen atom of Ala…”
mentioning
confidence: 99%