Gregori Aminoff Prize 2016

Poul Nissen (left) and Chikashi Toyoshima (right). Photos courtesy of The Royal Swedish Academy of Sciences.

The Royal Swedish Academy of Sciences has awarded the Gregori Aminoff Prize in crystallography 2016 to Poul Nissen, Aarhus U., Denmark, and Chikashi Toyoshima, U. of Tokyo, Japan. 'The prize winners have developed new technology to crystallize and determine the structure of membrane proteins in their natural environment. The major breakthrough is that these studies have broadened our understanding of the mechanism that transports ions through cell membranes, as well as the structural states that occur in this very complex system. Determination of the structure of membrane proteins has played a very important role in the development of modern medicine.' The prize includes 100.000SEK.

Paul Nissen, born in 1967, obtained his PhD at Aarhus U. in 1997 followed by a postdoctoral period at Yale U. In 2000 he returned to Aarhus U. where he is now Professor of Protein Biochemistry, as well as Director of the Danish Research Inst. of Translational Neuroscience and the PUMPkin Centre.

Chikashi Toyoshima, born in 1954, obtained his DSc degree in 1983 from U. of Tokyo, Japan. After a postdoctoral period at Stanford U., USA, and U. of Cambridge, UK, he returned in 1989 to Japan and is now Professor of Protein Biochemistry and Director of the Center for Bioinformatics at U. of Tokyo.

Professors Toyoshima and Nissen have determined crystal structures of several key members of the P-type ATPase family and established structures of essential intermediates in their ion transport cycles, information which has led to the detailed description of molecular mechanisms of these important ion translocation systems.

The P-type ATPases constitute a major family of membrane ion pumps found in all kingdoms of life. They catalyse the chemical-driven translocation of a range of different cations over biological membranes, including Ca²⁺, K⁺, Na⁺ and H⁺, as well as several transition and post-transition metals. The ion concentration gradients generated by P-type ATPases across biological membranes provide driving forces for many other biological processes, but also play prominent roles in cell signaling and regulation.

P-type ATPases are large multi-domain integral membrane proteins that undergo distinct conformational changes along the ion transport cycle and are therefore particularly challenging for crystallographic work. Toyoshima solved the first crystal structure of a P-type ATPase in 2000, the structure of the Ca⁺²-ATPase SERCA. To accomplish this he developed novel crystallization techniques allowing three-dimensional protein crystals to be grown within a phospholipid environment. He subsequently determined the SERCA Ca⁺²-ATPase structure in several trapped conformational states of the transport cycle. This work provided the initial description of the structural basis for ion transport by a P-type ATPase.

Nissen has also studied trapped conformational states of SERCA but in addition determined structures of P-type ATPases of other subfamilies including the Na⁺/K⁺, H⁺, and most recently copper and zinc P1B-type ATPases. His work also includes the development of novel strategies for trapping and crystallizing intermediates in the ion transport cycle of P-type ATPases. The independent and largely complementary work of these two scientists has led to fascinating insights into these molecular machines; the structural basis for the dramatic structural changes seen between different intermediates of the ion transport cycle; the sophisticated fine tuning of ion binding and release; the establishment of selectivity for specific ions; the dynamic formation of ion excite and entrance channels; and the molecular basis for how chemical energy from ATP is utilized to drive the structural transformations