Phosphorylation of movement proteins by the plasmodesmal-associated protein kinase.
Newark, United States. In Methods Mol Biol, 2007
Recently, we have reported the identification of a host protein kinase named plasmodesmal-associated protein kinase (PAPK) which specifically phosphorylates a subset of noncell autonomous proteins in vitro, including MPs of Tobacco mosaic virus (TMV) and Bean dwarf mosaic virus (BDMV).
Structural basis of chaperone function and pilus biogenesis.
Saint Louis, United States. In Science, 1999
The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation.
Structural polymorphism of bacterial adhesion pili.
Boston, United States. In Nature, 1995
They are attached to the outer membrane by a minor structural protein, PapH and are terminated by an approximately 20 A diameter fibrillus composed of PapK, PapE and PapF, which presents the host-binding adhesin PapG.