155C

THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550

155C の概要

• エントリーDOI: 10.2210/pdb155c/pdb
• 分子名称: CYTOCHROME C550, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Paracoccus denitrificans (Micrococcus denitrificans)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14891.75

構造登録者

Timkovich, R. (登録日: 1976-08-01, 公開日: 1976-08-20, 最終更新日: 2024-10-16)

主引用文献

Timkovich, R.,Dickerson, R.E.
The structure of Paracoccus denitrificans cytochrome c550.
J.Biol.Chem., 251:4033-4046, 1976

PubMed Abstract: The crystal structure of Paracoccus (formerly Micrococcus) denitrificans cytochrome c550 has been solved by x-ray diffraction to a resolution of 2.45 A. In both amino acid sequence and molecular structure it is evolutionarily homologous with mitochondrial cytochrome c from eukaryotes and photosynthetic cytochrome c2 from purple non-sulfur bacteria. All of these cytochromes c have the same basic folding pattern, with surface insertions of extra amino acids in c550. Various strains of c2 have all, some, or none of the extra insertions observed in c550. The hydrophobic heme environment, position of aromatic rings, and structure and environment of the heme crevice, are virtually identical in cytochromes c55o, c, and c2. Radical changes observed at all regions on the molecular surface except the heme crevice argue for the importance of the crevice and the exposed edge of the heme in the transfer of electrons to and from the cytochrome molecule.

PubMed: 180013

実験手法

X-RAY DIFFRACTION (2.5 Å)