1JDL
Structure of cytochrome c2 from Rhodospirillum Centenum
Summary for 1JDL
Entry DOI | 10.2210/pdb1jdl/pdb |
Descriptor | CYTOCHROME C2, ISO-2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | alpha helix, electron transport |
Biological source | Rhodospirillum centenum |
Total number of polymer chains | 1 |
Total formula weight | 13669.23 |
Authors | Camara-Artigas, A.,Williams, J.C.,Allen, J.P. (deposition date: 2001-06-14, release date: 2001-11-07, Last modification date: 2023-08-16) |
Primary citation | Camara-Artigas, A.,Williams, J.C.,Allen, J.P. Structure of cytochrome c2 from Rhodospirillum centenum. Acta Crystallogr.,Sect.D, 57:1498-1505, 2001 Cited by PubMed Abstract: Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed. PubMed: 11679712DOI: 10.1107/S0907444901010423 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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