< Eine eigene Proteinstruktur zum 50. Geburtstag

A personalized protein structure for a special birthday

Andrei N. Lupas receives his own personalized protein structure containing his name


Tuebingen, March 5, 2014.  Scientists from the Max Planck Institute for Developmental Biology in Tübingen, Germany, designed a protein structure with an amino acid sequence corresponding to the letters “Andrei N. Lupas”. The Director of the Department of Protein Evolution received the first personalized protein structure for his 50th birthday last year. The scientific work was already presented at the 6th Alpbach Coiled Coil Workshop in October 2013 and was now published online by the Journal of Structural Biology.

It took about four months until the researchers working with Marcus Hartmann and Birte Hernandez Alvarez from the Max Planck Institute for Developmental Biology, Department Protein Evolution, succeeded in incorporating the desired amino acid sequence into a protein and confirming the design by determining its structure experimentally. The results came just in time: Andrei N. Lupas received the first personalized protein structure as a surprise for his 50th birthday.

For their design, the researchers exploited the robustness of a part of the transcription factor GCN4, a so-called coiled coil, as a fusion adaptor. Coiled coils are structural elements of proteins that resemble the twisted strands of a rope and which exist in a vast variety of proteins in all forms of life. They consist of at least two α-helices, which are wound around each other and have an amino acid sequence that follows a periodic repeat pattern. In the simplest case, the heptad repeat, the pattern has seven positions. Due to distinct structural requirements, these positions have individual preferences for different kinds of amino acids.

In the present structure, the amino acid sequence “ANDREINLVPAS” was fused between two stabilizing GCN4 adaptors. “As the design was based on the heptad repeat, we had to take care that the individual amino acids of the inserted sequence match the requirements for their position in the sequence repeat pattern,” explains Marcus Hartmann. He and his colleagues chose a three-helical coiled coil as the basis because this seemed to be the best possibility to embed the letter N of Andrei within the coiled coil structure. The letter U was substituted by V as U does not exist in the amino acid alphabet.

A possible problem was posed by the letter P because its corresponding amino acid, proline, doesn’t really fit into α-helices. “Here we could only hope that we would end up with a reasonably folded structure,” says Hartmann. “At the end of the day we learned a lot about the accommodation of proline in coiled coils.” The actual structure was determined by X-ray crystallography.

Andrei N. Lupas himself has made significant contributions to the field of coiled coil research, thus unknowingly laying parts of the theoretical framework for his own birthday present – a personalized coiled coil specifically designed for him from scratch. Despite some imponderables like the accommodation of proline, the scientists succeeded with their design in the first attempt. The protein structure is now available in the Protein Data Bank (PDB). 

Original publication:

 

Deiss, S., et al. Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors. J. Struct. Biol. (2014), dx.doi.org/10.1016/j.jsb.2014.01.013


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The Max Planck Institute for Developmental Biology conducts basic research in the fields of biochemistry, genetics and evolutionary biology. It employs about 350 people and is located at the Max Planck Campus in Tübingen. The Max Planck Institute for Developmental Biology is one of 80 research institutes that the Max Planck Society for the Advancement of Science maintains in Germany.


The three-dimensional structure of the amino acid sequence „ANDREI-N-LVPAS“ inserted between two GCN4 adaptors is a three-helical coiled coil. Peculiarities of this structure are a bound bromide ion in the middle of the bundle and the accommodation of the amino acid proline (P), which is rarely found in natural coiled coils.

The three-dimensional structure of the amino acid sequence „ANDREI-N-LVPAS“ inserted between two GCN4 adaptors is a three-helical coiled coil. Peculiarities of this structure are a bound bromide ion in the middle of the bundle and the accommodation of the amino acid proline (P), which is rarely found in natural coiled coils.

Andrei Lupas

Andrei Lupas