1COT

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

Summary for 1COT

• Entry DOI: 10.2210/pdb1cot/pdb
• Descriptor: CYTOCHROME C2, HEME C (3 entities in total)
• Functional Keywords: electron transport
• Biological source: Paracoccus denitrificans
• Total number of polymer chains: 1
• Total formula weight: 14461.06

Authors

Benning, M.M.,Meyer, T.E.,Holden, H.M. (deposition date: 1994-07-06, release date: 1994-09-30, Last modification date: 2021-03-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)