155c
From Proteopedia
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|PDB= 155c |SIZE=350|CAPTION= <scene name='initialview01'>155c</scene>, resolution 2.5Å | |PDB= 155c |SIZE=350|CAPTION= <scene name='initialview01'>155c</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=155c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=155c OCA], [http://www.ebi.ac.uk/pdbsum/155c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=155c RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Timkovich, R.]] | [[Category: Timkovich, R.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: HEM]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:25 2008'' |
Revision as of 15:28, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
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