1YNR: Crystal Structure Of The Cytochrome C-552 From Hydrogenobacter Thermophilus At 2.0 Resolution

The folding mechanism of many proteins involves the population of partially organized structures en route to the native state. Identification and characterization of these intermediates is particularly difficult, as they are often only transiently populated and may play different mechanistic roles, being either on-pathway productive species or off-pathway kinetic traps. Following different spectroscopic probes, and employing state-of-the-art kinetic analysis, we present evidence that the folding mechanism of the thermostable cytochrome c552 from Hydrogenobacter thermophilus does involve the presence of an elusive, yet compact, on-pathway intermediate. Characterization of the folding mechanism of this cytochrome c is particularly interesting for the purpose of comparative folding studies, because H. thermophilus cytochrome c552 shares high sequence identity and structural homology with its homologue from the mesophilic bacterium Pseudomonas aeruginosa cytochrome c551, which refolds through a broad energy barrier without the accumulation of intermediates. Analysis of the folding kinetics and correlation with the three-dimensional structure add new evidence for the validity of a consensus folding mechanism in the cytochrome c family.
PDB ID: 1YNRDownload
MMDB ID: 33358
PDB Deposition Date: 2005/1/25
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1YNR: tetrameric; determined by author and by software (PISA)
Molecular Components in 1YNR
Label Count Molecule
Proteins (4 molecules)
Cytochrome C-552
Molecule annotation
Chemicals (15 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB