2JQR
Solution model of crosslinked complex of cytochrome c and adrenodoxin
Summary for 2JQR
| Entry DOI | 10.2210/pdb2jqr/pdb |
| Related | 1AYF 1YCC |
| NMR Information | BMRB: 7390,15301 |
| Descriptor | Cytochrome c iso-1, Adrenodoxin, mitochondrial, HEME C, ... (4 entities in total) |
| Functional Keywords | electron transport, cytochrome c, adrenodoxin, crosslinked complex, 2fe2s ferredoxin, pseudocontact shift, paramagnetic relaxation enhancement, encounter complex |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Mitochondrion intermembrane space: P00044 Mitochondrion matrix: P00257 |
| Total number of polymer chains | 2 |
| Total formula weight | 24505.26 |
| Authors | Xu, X.,Reinle, W.,Hannemann, F.,Konarev, P.V.,Svergun, D.I.,Bernhardt, R.,Ubbink, M. (deposition date: 2007-06-07, release date: 2008-04-22, Last modification date: 2024-10-30) |
| Primary citation | Xu, X.,Reinle, W.,Hannemann, F.,Konarev, P.V.,Svergun, D.I.,Bernhardt, R.,Ubbink, M. Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy J.Am.Chem.Soc., 130:6395-6403, 2008 Cited by PubMed Abstract: In the general view of protein-complex formation, a transient and dynamic encounter complex proceeds to form a more stable, well-defined, and active form. In weak protein complexes, however, the encounter state can represent a significant population of the complex. The redox proteins adrenodoxin (Adx) and cytochrome c (C c) associate to form such a weak and short-lived complex, which is nevertheless active in electron transfer. To study the conformational freedom within the protein complex, the native complex has been compared to a cross-linked counterpart by using solution scattering and NMR spectroscopy. Oligomerization behavior of the native complex in solution revealed by small-angle X-ray scattering indicates a stochastic nature of complex formation. For the cross-linked complex, interprotein paramagnetic effects are observed, whereas for the native complex, extensive averaging occurs, consistent with multiple orientations of the proteins within the complex. Simulations show that C c samples about half of the surface area of adrenodoxin. It is concluded that the complex of Adx/C c is entirely dynamic and can be considered as a pure encounter complex. PubMed: 18439013DOI: 10.1021/ja7101357 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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