2RDV
RUBREDOXIN FROM DESULFOVIBRIO VULGARIS MIYAZAKI F, MONOCLINIC CRYSTAL FORM
Summary for 2RDV
Entry DOI | 10.2210/pdb2rdv/pdb |
Descriptor | RUBREDOXIN, FE (III) ION (3 entities in total) |
Functional Keywords | rubredoxin, compnd, electron transfer protein, metalloprotein, sulfate-reducing bacterium, electron transfer |
Biological source | Desulfovibrio vulgaris str. 'Miyazaki F' |
Cellular location | Cytoplasm: P15412 |
Total number of polymer chains | 3 |
Total formula weight | 16974.25 |
Authors | Higuchi, Y.,Yasuoka, N. (deposition date: 1998-10-07, release date: 1999-05-18, Last modification date: 2024-05-22) |
Primary citation | Misaki, S.,Morimoto, Y.,Ogata, M.,Yagi, T.,Higuchi, Y.,Yasuoka, N. Structure determination of rubredoxin from Desulfovibrio vulgaris Miyazaki F in two crystal forms. Acta Crystallogr.,Sect.D, 55:408-413, 1999 Cited by PubMed Abstract: The structures of two crystal forms (form I, P3221, a = b = 43.7, c = 50.7 A; form II, P21, a = 27.3, b = 44.9, c = 51.2 A and beta = 90. 6 degrees ) of the rubredoxin from Desulfovibrio vulgaris Miyazaki F have been solved by the molecular-replacement method. Form I has been refined at a resolution of 2.0 A to an R value of 20.8% and includes 32 water molecules. Form II includes 86 water molecules and has been refined at 1.9 A resolution to an R value of 17.5%. In form II, there are three molecules in the asymmetric unit with the molecules related by a non-crystallographic 32 symmetry axis. In both crystal forms, it was found that only a few residues effectively participate in the formation of intermolecular contacts along both the crystallographic (form I) and the non-crystallographic (form II) 32 axes. The crystal structure of the form II crystal is compared with those of other rubredoxin molecules from anaerobic bacteria. From this comparison, a similarity in the core region, which is composed of aromatic residues and includes the active centre, has been revealed. PubMed: 10089348DOI: 10.1107/S0907444998011810 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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