|
|
| Line 1: |
Line 1: |
| [[Image:2o98.gif|left|200px]] | | {{Seed}} |
| | [[Image:2o98.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2o98| PDB=2o98 | SCENE= }} | | {{STRUCTURE_2o98| PDB=2o98 | SCENE= }} |
|
| |
|
| '''Structure of the 14-3-3 / H+-ATPase plant complex'''
| | ===Structure of the 14-3-3 / H+-ATPase plant complex=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| Regulatory 14-3-3 proteins activate the plant plasma membrane H(+)-ATPase by binding to its C-terminal autoinhibitory domain. This interaction requires phosphorylation of a C-terminal, mode III, recognition motif as well as an adjacent span of approximately 50 amino acids. Here we report the X-ray crystal structure of 14-3-3 in complex with the entire binding motif, revealing a previously unidentified mode of interaction. A 14-3-3 dimer simultaneously binds two H(+)-ATPase peptides, each of which forms a loop within the typical 14-3-3 binding groove and therefore exits from the center of the dimer. Several H(+)-ATPase mutants support this structure determination. Accordingly, 14-3-3 binding could result in H(+)-ATPase oligomerization. Indeed, by using single-particle electron cryomicroscopy, the 3D reconstruction of the purified H(+)-ATPase/14-3-3 complex demonstrates a hexameric arrangement. Fitting of 14-3-3 and H(+)-ATPase atomic structures into the 3D reconstruction map suggests the spatial arrangement of the holocomplex.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17289589}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17289589 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17289589}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| [[Category: Protein binding]] | | [[Category: Protein binding]] |
| [[Category: Regulation]] | | [[Category: Regulation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:54:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:37:48 2008'' |
