2O98

Structure of the 14-3-3 / H+-ATPase plant complex

Summary for 2O98

• Entry DOI: 10.2210/pdb2o98/pdb
• Descriptor: 14-3-3-like protein C, Plasma membrane H+ ATPase, SULFATE ION, ... (5 entities in total)
• Functional Keywords: h, atpase, 14-3-3, plasma membrane, electrochemical proton gradient, cell turgor, regulation, protein binding
• Biological source: Nicotiana tabacum (common tobacco); More
• Total number of polymer chains: 4
• Total formula weight: 68499.28

Authors

Ottmann, C.,Weyand, M.,Wittinghofer, A.,Oecking, C. (deposition date: 2006-12-13, release date: 2007-04-03, Last modification date: 2023-12-27)

Primary citation

Ottmann, C.,Marco, S.,Jaspert, N.,Marcon, C.,Schauer, N.,Weyand, M.,Vandermeeren, C.,Duby, G.,Boutry, M.,Wittinghofer, A.,Rigaud, J.L.,Oecking, C.
Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+ -ATPase by combining X-ray crystallography and electron cryomicroscopy
Mol.Cell, 25:427-440, 2007

PubMed Abstract: 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.

PubMed: 17289589
DOI: 10.1016/j.molcel.2006.12.017

Experimental method

X-RAY DIFFRACTION (2.7 Å)