1COT

X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION

1COT の概要

• エントリーDOI: 10.2210/pdb1cot/pdb
• 分子名称: CYTOCHROME C2, HEME C (3 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Paracoccus denitrificans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14461.06

構造登録者

Benning, M.M.,Meyer, T.E.,Holden, H.M. (登録日: 1994-07-06, 公開日: 1994-09-30, 最終更新日: 2024-11-20)

主引用文献

Benning, M.M.,Meyer, T.E.,Holden, H.M.
X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution.
Arch.Biochem.Biophys., 310:460-466, 1994

PubMed Abstract: The cytochrome c2 (formerly c550) isolated from Paracoccus denitrificans is one of the larger bacterial c-type proteins examined thus far. The molecular structure of this cytochrome has been redetermined and refined to 1.7-A resolution with a crystallographic R-factor of 17.5% for all measured X-ray data. Like other, smaller c-type cytochromes, the molecule consists of five alpha-helices that wrap around the heme group. In addition, this bacterial cytochrome contains two strands of anti-parallel beta-sheet, five Type I turns, and three Type II turns. The present model differs from the originally determined structure in several regions including the N-terminus, the loop delineated by Asp 25 to Lys 31, the region defined by Trp 86 to Val 88, and the C-terminus. A total of 103 water molecules has been positioned into the electron density map. Six of these waters are directly involved in heme binding.

PubMed: 8179333
DOI: 10.1006/abbi.1994.1193

実験手法

X-RAY DIFFRACTION (1.7 Å)