2B4Z
Crystal structure of cytochrome C from bovine heart at 1.5 A resolution.
Summary for 2B4Z
Entry DOI | 10.2210/pdb2b4z/pdb |
Descriptor | Cytochrome c, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | ferric form, low ionic strength, electron transport |
Biological source | Bos taurus (cattle) |
Cellular location | Mitochondrion matrix: P62894 |
Total number of polymer chains | 1 |
Total formula weight | 12211.88 |
Authors | Mirkin, N.,Jakoncic, J.,Stojanoff, V.,Moreno, A. (deposition date: 2005-09-27, release date: 2005-10-11, Last modification date: 2023-08-23) |
Primary citation | Mirkin, N.,Jaconcic, J.,Stojanoff, V.,Moreno, A. High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor. Proteins, 70:83-92, 2008 Cited by PubMed Abstract: Cytochrome c is one of the most studied proteins probably due to its electron-transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, M(r) 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well-studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 A resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented. PubMed: 17634981DOI: 10.1002/prot.21452 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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