3CP5

Cytochrome c from rhodothermus marinus

Summary for 3CP5

• Entry DOI: 10.2210/pdb3cp5/pdb
• Descriptor: Cytochrome c, SULFATE ION, HEME C, ... (4 entities in total)
• Functional Keywords: cytochrome c, electron transfer protein, electron transport
• Biological source: Rhodothermus marinus (Rhodothermus obamensis)
• Total number of polymer chains: 1
• Total formula weight: 14549.30

Authors

Stelter, M.,Melo, A.,Saraiva, L.,Teixeira, M.,Archer, M. (deposition date: 2008-03-31, release date: 2008-10-28, Last modification date: 2024-10-30)

Primary citation

Stelter, M.,Melo, A.M.,Pereira, M.M.,Gomes, C.M.,Hreggvidsson, G.O.,Hjorleifsdottir, S.,Saraiva, L.M.,Teixeira, M.,Archer, M.
A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c
Biochemistry, 47:11953-11963, 2008

PubMed Abstract: Monoheme cytochromes of the C-type are involved in a large number of electron transfer processes, which play an essential role in multiple pathways, such as respiratory chains, either aerobic or anaerobic, and the photosynthetic electron transport chains. This study reports the biochemical characterization and the crystallographic structure, at 1.23 A resolution, of a monoheme cytochrome c from the thermohalophilic bacterium Rhodothermus marinus. In addition to an alpha-helical core folded around the heme, common for this type of cytochrome, the X-ray structure reveals one unusual alpha-helix and a unique N-terminal extension, which wraps around the back of the molecule. Based on a thorough structural and amino acid sequence comparison, we propose R. marinus cytochrome c as the first characterized member of a new class of C-type cytochromes.

PubMed: 18855424
DOI: 10.1021/bi800999g

Experimental method

X-RAY DIFFRACTION (1.24 Å)