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1cot

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{{STRUCTURE_1cot| PDB=1cot | SCENE= }}
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'''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION'''
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===X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8179333}}
==About this Structure==
==About this Structure==
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[[Category: Meyer, T E.]]
[[Category: Meyer, T E.]]
[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:02:10 2008''

Revision as of 18:02, 30 June 2008

Image:1cot.png

Template:STRUCTURE 1cot

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

Template:ABSTRACT PUBMED 8179333

About this Structure

1COT is a Single protein structure of sequence from Paracoccus denitrificans. 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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