155c
From Proteopedia
(New page: 200px<br /><applet load="155c" size="450" color="white" frame="true" align="right" spinBox="true" caption="155c, resolution 2.5Å" /> '''THE STRUCTURE OF PARA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:155c.jpg|left|200px]]<br /><applet load="155c" size=" | + | [[Image:155c.jpg|left|200px]]<br /><applet load="155c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="155c, resolution 2.5Å" /> | caption="155c, resolution 2.5Å" /> | ||
'''THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550'''<br /> | '''THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Paracoccus (formerly Micrococcus) denitrificans | + | The crystal structure of Paracoccus (formerly Micrococcus) denitrificans cytochrome c550 has been solved by x-ray diffraction to a resolution of 2.45 A. In both amino acid sequence and molecular structure it is evolutionarily homologous with mitochondrial cytochrome c from eukaryotes and photosynthetic cytochrome c2 from purple non-sulfur bacteria. All of these cytochromes c have the same basic folding pattern, with surface insertions of extra amino acids in c550. Various strains of c2 have all, some, or none of the extra insertions observed in c550. The hydrophobic heme environment, position of aromatic rings, and structure and environment of the heme crevice, are virtually identical in cytochromes c55o, c, and c2. Radical changes observed at all regions on the molecular surface except the heme crevice argue for the importance of the crevice and the exposed edge of the heme in the transfer of electrons to and from the cytochrome molecule. |
==About this Structure== | ==About this Structure== | ||
| - | 155C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 155C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=155C OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:38:26 2008'' |
Revision as of 09:38, 21 February 2008
|
THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550
Overview
The crystal structure of Paracoccus (formerly Micrococcus) denitrificans cytochrome c550 has been solved by x-ray diffraction to a resolution of 2.45 A. In both amino acid sequence and molecular structure it is evolutionarily homologous with mitochondrial cytochrome c from eukaryotes and photosynthetic cytochrome c2 from purple non-sulfur bacteria. All of these cytochromes c have the same basic folding pattern, with surface insertions of extra amino acids in c550. Various strains of c2 have all, some, or none of the extra insertions observed in c550. The hydrophobic heme environment, position of aromatic rings, and structure and environment of the heme crevice, are virtually identical in cytochromes c55o, c, and c2. Radical changes observed at all regions on the molecular surface except the heme crevice argue for the importance of the crevice and the exposed edge of the heme in the transfer of electrons to and from the cytochrome molecule.
About this Structure
155C is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of Paracoccus denitrificans cytochrome c550., Timkovich R, Dickerson RE, J Biol Chem. 1976 Jul 10;251(13):4033-46. PMID:180013
Page seeded by OCA on Thu Feb 21 11:38:26 2008
