| Title: | Structural evidence for the functional importance of the heme domain mobility in flavocytochrome b2. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1024999 |
| landingPage: |
http://www.iedb.org/assay/1967705 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2010
|
| study type: | b cell assays |
| subject species: | Saccharomyces cerevisiae S288C |
| fullName: |
K H Diê
p Lê
Florence Lederer
Bé
atrice Golinelli-Pimpaneau
|
| method: |
x-ray crystallography
|
| name: |
Structural evidence for the functional importance of the heme domain mobility in flavocytochrome b2.
|
| description: |
The epitope of B2B4 Fab on the Fcb2 heme domain carrying protoporphyrin IX (Fe) was determined from the crystal structure of the complex, solved by molecular replacement. The asymmetric unit contains two heme domains and two Fab molecules. The two molecules have nearly identical structures and very similar B-factors. The head-to-tail arrangement of the two complexes (Fig. 1a) results in the heme domain being sandwiched between the combining site of one Fab and the constant light chain of the other one. Region H128–H133 in CH1, which belongs to a loop that is disordered in most Fab crystal structures, was not modeled.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |