1kyo
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1kyo.gif|left|200px]] | [[Image:1kyo.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1kyo", 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_1kyo| PDB=1kyo | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C''' | '''YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C''' | ||
| Line 30: | Line 27: | ||
[[Category: Hunte, C.]] | [[Category: Hunte, C.]] | ||
[[Category: Lange, C.]] | [[Category: Lange, C.]] | ||
| - | [[Category: | + | [[Category: Antibody fv fragment mediated crystallization]] |
| - | [[Category: | + | [[Category: Electron transfer complex]] |
| - | [[Category: | + | [[Category: Enzyme substrate complex]] |
| - | [[Category: | + | [[Category: Multisubunit membrane protein complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:19:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:19, 2 May 2008
YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C
Overview
Small diffusible redox proteins facilitate electron transfer in respiration and photosynthesis by alternately binding to integral membrane proteins. Specific and transient complexes need to be formed between the redox partners to ensure fast turnover. In respiration, the mobile electron carrier cytochrome c shuttles electrons from the cytochrome bc1 complex to cytochrome c oxidase. Despite extensive studies of this fundamental step of energy metabolism, the structures of the respective electron transfer complexes were not known. Here we present the crystal structure of the complex between cytochrome c and the cytochrome bc1 complex from Saccharomyces cerevisiae. The complex was crystallized with the help of an antibody fragment, and its structure was determined at 2.97-A resolution. Cytochrome c is bound to subunit cytochrome c1 of the enzyme. The tight and specific interactions critical for electron transfer are mediated mainly by nonpolar forces. The close spatial arrangement of the c-type hemes unexpectedly suggests a direct and rapid heme-to-heme electron transfer at a calculated rate of up to 8.3 x 10(6) s(-1). Remarkably, cytochrome c binds to only one recognition site of the homodimeric multisubunit complex. Interestingly, the occupancy of quinone in the Qi site is higher in the monomer with bound cytochrome c, suggesting a coordinated binding and reduction of both electron-accepting substrates. Obviously, cytochrome c reduction by the cytochrome bc1 complex can be regulated in response to respiratory conditions.
About this Structure
1KYO is a Protein complex structure of sequences from Mus musculus and Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1KYO with [Cytochrome c]. Full crystallographic information is available from OCA.
Reference
Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c., Lange C, Hunte C, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2800-5. PMID:11880631 Page seeded by OCA on Fri May 2 23:19:47 2008
