Previously, gp16, the ATPase protein of phi29 DNA packaging motor, was an enigma due to its tendency to form multiple oligomeric states. Recently we employed new methodologies to decipher both its stoichiometry and also the mechanism in which the protein functions to hydrolyze ATP and provide the driving force for DNA packaging. The oligomeric states were determined by biochemical and biophysical approaches. Contrary to many reported intriguing models of viral DNA packaging, it was found that phi29 DNA packaging motor permits the translocation of DNA unidirectionally and driven cooperatively by three rings of defined shape. The mechanism for the generation of force and the role of adenosine and phosphate in motor motion were demonstrated. It was concluded that phi29 genomic DNA is pushed to traverse the motor channel section by section with the aid of ATPase gp16, similar to the hexameric AAA+ family in the translocation of dsDNA. A new model of "Push through a One-way Valve" for the mechanism of viral DNA packaging motor was coined to describe the coordinated interaction among the hexameric packaging ATPase gp16 and the revolution mechanism of the dodecameric channel which serves as a control device to regulate the directional movement of dsDNA.