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Alumni Association News 2010

11 June 2010

John Kendrew Award Winner: Preben Morth

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Niovi Santama, Preben Morth and Paul Tucker at the John Kendrew Award Ceremony

John Kendrew Award Ceremony

Selection of Winner

On Preben's science in Oslo

About the John Kendrew Award

Award Ceremony

On 11 June 2010, the John Kendrew Young Scientist Award winner Preben Morth, was presented with his medal by his former group leader Paul Tucker. Paul, now retired, was a group leader in the Structural and Computational Biology unit at EMBL Hamburg (1984-2009) and presented the award on behalf of the EMBL Pensioner’s Association.

Niovi Santama, Deputy Vice Chair of the EMBL Alumni Association (EAA), and Associate Professor at the University of Cyprus, introduced Preben to an enthusiastic audience. His presentation, titled “There and back again” (in honour of the crystallographer’s favourite read - Lord of the Rings), was well received. It introduced listeners to Aarhus University, structural biology, and his team’s own project “A pumps tail” where he outlined how they:

  • solved the structure of the sodium pump, trapped in the E2(Rb/K)2MgF4 Form,
  • located the position of the transmembrane β and γ chain,
  • identified a regulatory role of the C-terminus, a switch possibly controlled by the membrane potential and
  • located and describe the potassium binding sites.


This work was published in 2007 in Nature and was the basis for his team’s more recent publication (see recent successes).

Preben and his student Kaare Andersen said lab day, held in the new ATC building, was very enjoyable. They found the building impressive and remarked that there was an “excitement for science buzzing in the air” everywhere they looked and went.

Selection of winner

The selection committee was again faced with an exceptionally difficult decision based on the outstanding quality of applications, but after a long discussion at their meeting on 14 December, Preben Morth, a PhD student in Paul Tucker’s group at EMBL Hamburg from 2001 to 2005 emerged as the winner.

“Our decision was based on his outstanding contribution, especially since leaving EMBL, to the structural biology of membrane proteins,” says EMBL Alumni Association chair Giulio Superti-Furga. “He has also been a real inspiration to school students with his enthusiastic involvement in science education.”

Preben, who is the first outstation scientist to win the award, was associate professor at Aarhus University in his native Denmark at the time the award was decided. “I am incredibly proud to have received it,” he says. “John Kendrew was one of the founding fathers of protein crystallography, and to have received an award that carries his name will always stand out as an absolute highlight of my career.”

Preben deserves particular recognition for solving the structure of sodium potassium ATPase, or sodium pump for short, an enzyme found in the plasma membrane of all animals. “Nobel laureate Jens Christian Skou – another Dane – discovered the sodium pump more than 50 years ago,” he says. “During my postdoc I pushed my project from initial crystals to the complete determination of the structure. The work taught me to keep going even when success seemed unachievable. The foundation for my interest and for structural biology was laid at EMBL Hamburg, studying bacterial two-components systems.”

The selection committee would like to thank all applicants and wish them every success for the future. Thanks also to EMBL faculty members for the nominations, and Halldór Stefánsson and Kai Simons for their advice.

On Preben's science in Oslo

On October 1st this years John Kendrew Award (JKA) Winner 2010, Preben Morth, started as a researcher at the Centre for Molecular Medicine Norway based in Oslo. He is currently building his team in Oslo and is full of enthusiasm for the challenges ahead.

He and his team recently published a paper (Nature: 467, 99–102, September 2010) that describes how they combined structural analysis with electrophysiological data and atomic simulation, to establish the existence of a novel ion pathway in the Na,K ATPase.

The interpretation of the combined data material reveal a, so far, novel model for ion translocation possible for the Na,K ATPase. This builds on his earlier success in solving the structure of sodium potassium ATPase, or sodium pump for short, an enzyme found in the plasma membrane of all animals and for was one of the reasons he won the JKA award.

The Morth group focuses on a structural systems biology approach to anion transporters involved in the acid/base homeostasis. They seek to understand the molecular mechanism involved with bicarbonate transport across the cell membrane. Bicarbonate transporters are grouped in two major classes the solute carrier family 4 (SLC4) and 26 (SLC26), the latter family is often associated with sulfate transport as well. They will also continue ongoing projects which focus on calcium and magnesium transporters, belonging to the P-type ATPases from bacterial systems. They have also shown to be directly involved with pH regulation since they often use protons as counterions.