155c: Difference between revisions

Revision as of 15:32, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:155c.png

Template:STRUCTURE 155c

THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550

Template:ABSTRACT PUBMED 180013

About this StructureAbout this Structure

155C is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

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 Mon Jun 30 15:32:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:155c.jpg|left|200px]]
+{{Seed}}
+[[Image:155c.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_155c|  PDB=155c  |  SCENE=  }}
-'''THE STRUCTURE OF PARACOCCUS DENITRIFICANS CYTOCHROME C550'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_180013}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 180013 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_180013}}
 ==About this Structure==
@@ Line 23: / Line 27: @@
 [[Category: Timkovich, R.]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:31:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:32:07 2008''