1cyc
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1cyc.gif|left|200px]] | [[Image:1cyc.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1cyc", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1cyc| PDB=1cyc | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION''' | '''THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION''' | ||
| Line 30: | Line 27: | ||
[[Category: Tsukihara, T.]] | [[Category: Tsukihara, T.]] | ||
[[Category: Yamane, T.]] | [[Category: Yamane, T.]] | ||
| - | [[Category: | + | [[Category: Electron transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:14:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:14, 2 May 2008
THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION
Overview
The structure analysis of bonito heart ferrocytochrome c was carried out at 2.3 A resolution by X-ray diffraction, and a Kendrew-type skeletal model was built up. This molecule has an overall egg shape, 35 A in height, 30 A in width and 23 A in thickness; the 5th ligand of the heme iron atom is the N-epsilon atom of the His-18 imidazole ring and the 6th is the Met-80 sulfur atom. Distinct alpha-helix regions are found between the N-terminus and reside 11, between 60 and 69, and between 90 and the C-terminus. The most distinct difference between the conformation of the present molecule and that of the horse oxidized molecule is the location of the Phe-82 phenyl ring. In the present reduced molecule, the phyenyl ring is in closer contact with the iron atom and gives influences on the character of the iron atom. Inside the molecule, at the lower part of the heme pocket, there is an extended hydrogen bond network including the propionic acid residues of the heme group. Both Phe-82 and the hydrogen bond network may play a key role in the function of this molecule.
About this Structure
1CYC is a Single protein structure of sequence from Katsuwonus pelamis. Full crystallographic information is available from OCA.
Reference
The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function., Tanaka N, Yamane T, Tsukihara T, Ashida T, Kakudo M, J Biochem. 1975 Jan 1;77(1?):147-62. PMID:166072 Page seeded by OCA on Fri May 2 13:14:34 2008
