Tag: protein complexes

Scientists develop strategy to engineer artificial allosteric sites in protein complexes

Scientists develop strategy to engineer artificial allosteric sites in protein complexes

According to a recently published research paper by a team of scientists, a groundbreaking approach has been developed to create artificial allosteric sites (where by binding an effector molecule, activity at the distal active site is regulated) in protein complexes. This breakthrough research holds significant promise for a wide range of applications in industrial, biological, medical, and agricultural fields.

The team’s work is published in Nature Chemistry on 06 July 2023 at 16:00 (London time).


Protein complexes, such as hemoglobin and molecular motors, exert concerted functions through cooperative work between the subunits (constituent proteins in the protein complex). This orchestration is enabled by the allosteric mechanism. The allosteric effect, regulation of function at an active site in a subunit by the binding of an effector molecule to an allosteric site in another subunit, was originally proposed in the 1960s and since then it has remained one of the most important topics in the biochemistry field. The research team developed a strategy for designing artificial allosteric sites into protein complexes to regulate a concerted function of a protein complex. “The creation of artificial allosteric sites into protein complexes has the potential to reveal fundamental principles for allostery and serve as tools for synthetic biology,” said Nobuyasu Koga, a professor at the Osaka University.


The research team hypothesized that allosteric sites in protein complexes can be created by restoring lost functions of the pseudo-active sites which are predicted to have been lost during evolution. Various protein complexes include subunits that have pseudo-active sites. It has been
reported that pseudo-active sites have an allosteric connection with active sites in other subunits. For example, a pseudo-active site in a subunit, which has lost ATPase activity but still exhibits ATP-binding ability, activates another subunit’s active site upon binding to ATP. (At the cellular
level, ATP is the source of energy. ATPase describes the enzyme’s ability to decompose ATP.) Such studies support the idea that distinct allosteric sites can be created into protein complexes by engineering pseudo-active sites.

Read more on the Photon Factory website

Image: Fig. 1 Design of allosteric sites into a rotary molecular motor

New electron microscope centre to advance research into structural biology and new materials

New electron microscope centre to advance research into structural biology and new materials

  • This cutting-edge facility will house two high-end electron microscopes: one to determine the structure of large protein complexes and another to study materials at atomic level.
  • Created thanks to the joint effort of several research institutes, the centre is located at the ALBA Synchrotron and will be open to the entire scientific community.
  • Catalan Research and Universities Minister Joaquim Nadal inaugurated the centre, which has received funding from the Catalan Government’s ERDF programme, on 24 February.

The Joint Electron Microscopy Center at ALBA (JEMCA) was created thanks to the collaboration of different research entities to launch a new centre within the ALBA Synchrotron building offering electron microscope services to the scientific community. In specific, eight different partners will be using this centre: the Institute for Molecular Biology of Barcelona (IBMB-CSIC), the Catalan Institute for Nanoscienc and Nanotechnology (ICN2), the Institute for Biomedical Research (IRB Barcelona), the Centre for Genome Regulation (CRG), the Institute for Materials Science of Barcelona (ICMAB-CSIC), the Spanish National Research Council (CSIC), the Universitat Autònoma de Barcelona (UAB), and the ALBA Synchrotron. The project definition phase also included the fundamental support of the Barcelona Institute of Science and Technology (BIST).

This is the only facility in all of Spain that allows working with tools that are complementary to the synchrotron light source with the aim of gathering more information in the field of structural biology and materials science.

The centre currently houses two microscopes: the Cryo-TEM, coordinated by the Institute for Molecular Biology of Barcelona (IBMB-CSIC), and the METCAM, coordinated by the Catalan Institute for Nanoscience and Nanotechnology (ICN2).

The Cryo-TEM microscope is key to being able to solve rapidly and with high resolution the protein structures that cannot be analysed with other techniques. This microscope is already being put to use in experiments with an elevated social return. For example, IBMB-CSIC researchers Núria Verdaguer and Pablo Guerra, in collaboration with IRB Barcelona researchers Manuel Palacín and David Aparicio and the spin-off Ona Therapeutics, are analysing a protein involved in metastatic lung cancer as well as the protein’s complex with an antibody of interest for a therapy that targets metastases. The Cryo-TEM is the second microscope of its kind in Spain and represents a great advance for the user community in this field.

Read more on the ALBA website