1cot
X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION
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Overview
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.
About this Structure
1COT is a Single protein structure of sequence from Paracoccus denitrificans with HEM as ligand. Full crystallographic information is available from OCA.
Reference
X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:8179333
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