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Arch Biochem Biophys. 1994 May 1;310(2):460-6.

X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution.

Author information

1
Institute for Enzyme Research, Graduate School, University of Wisconsin, Madison 53705.

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.

PMID:
8179333
DOI:
10.1006/abbi.1994.1193
[Indexed for MEDLINE]

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