3VNW
Crystal structure of cytochrome c552 from Thermus thermophilus at pH 5.44
Summary for 3VNW
Entry DOI | 10.2210/pdb3vnw/pdb |
Descriptor | Cytochrome c-552, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | cytochrome c, electron transfer, electron transport |
Biological source | Thermus thermophilus |
Total number of polymer chains | 1 |
Total formula weight | 14611.85 |
Authors | Yamada, S.,Bouley-Ford, N.D.,Keller, G.E.,Winkler, J.R.,Gray, H.B. (deposition date: 2012-01-18, release date: 2013-01-23, Last modification date: 2023-11-08) |
Primary citation | Yamada, S.,Bouley-Ford, N.D.,Keller, G.E.,Ford, W.C.,Gray, H.B.,Winkler, J.R. Snapshots of a protein folding intermediate Proc.Natl.Acad.Sci.USA, 110:1606-1610, 2013 Cited by PubMed Abstract: We have investigated the folding dynamics of Thermus thermophilus cytochrome c(552) by time-resolved fluorescence energy transfer between the heme and each of seven site-specific fluorescent probes. We have found both an equilibrium unfolding intermediate and a distinct refolding intermediate from kinetics studies. Depending on the protein region monitored, we observed either two-state or three-state denaturation transitions. The unfolding intermediate associated with three-state folding exhibited native contacts in β-sheet and C-terminal helix regions. We probed the formation of a refolding intermediate by time-resolved fluorescence energy transfer between residue 110 and the heme using a continuous flow mixer. The intermediate ensemble, a heterogeneous mixture of compact and extended polypeptides, forms in a millisecond, substantially slower than the ∼100-μs formation of a burst-phase intermediate in cytochrome c. The surprising finding is that, unlike for cytochrome c, there is an observable folding intermediate, but no microsecond burst phase in the folding kinetics of the structurally related thermostable protein. PubMed: 23319660DOI: 10.1073/pnas.1221832110 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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