Structural similarity of cytochrome c2 from Rhodopseudomonas viridis to mitochondrial cytochromes c revealed by its crystal structure at 2.7 A resolution.
The crystal structure of cytochrome c2 from Rhodopseudomonas viridis has been refined using molecular dynamics and restrained least-squares methods to a crystallographic R-factor of 0.216 at 2.7 A resolution. A structural comparison between Rps. viridis cytochrome c2 and the other bacterial cytochromes c2 or mitochondrial cytochromes c indicates that the overall protein foldings are very similar to each other with the exception of the surface loop and terminal region of the polypeptide chain. However, the position and hydrogen-bond pattern of the evolutionarily conserved water molecule buried within the heme binding pocket in Rps. viridis cytochrome c2 are common to those in the mitochondrial cytochromes c. This fact indicates that Rps. viridis cytochrome c2 is structurally more similar to mitochondrial cytochromes c than to the other bacterial cytochromes c2.
Sogabe
S
S
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Japan.
Ezoe
T
T
Kasai
N
N
Saeda
M
M
Uno
A
A
Miki
M
M
Miki
K
K
D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry*; D045362:Cytochromes c2; D006418:Heme / Q000737:chemistry; D006860:Hydrogen Bonding; D008928:Mitochondria / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D012241:Rhodopseudomonas / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D003574:Cytochrome c Group; D014867:Water; D006418:Heme; D045362:Cytochromes c2