1cot
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(New page: 200px<br /><applet load="1cot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cot, resolution 1.7Å" /> '''X-RAY STRUCTURE OF TH...)
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Revision as of 10:30, 20 November 2007
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X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION
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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