1cot: Difference between revisions

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New page: left|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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[[Image:1cot.jpg|left|200px]]<br /><applet load="1cot" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1cot, resolution 1.7&Aring;" />
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'''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION'''<br />
'''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1COT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1COT OCA].  
1COT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COT OCA].  


==Reference==
==Reference==
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[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Benning, M.M.]]
[[Category: Benning, M M.]]
[[Category: Holden, H.M.]]
[[Category: Holden, H M.]]
[[Category: Meyer, T.E.]]
[[Category: Meyer, T E.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: electron transport]]
[[Category: electron transport]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:38:03 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:11 2008''

Revision as of 13:08, 21 February 2008

File:1cot.jpg


1cot, resolution 1.7Å

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

OverviewOverview

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 StructureAbout this Structure

1COT is a Single protein structure of sequence from Paracoccus denitrificans with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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