The biopolymer has far-reaching potential from medical therapeutics to replacing synthetic plastics. Armed with a deep understanding of how the enzymes makes acholetin, scientists now have a target for preventing bacterial contamination and the means to produce acholetin for a variety of purposes.
For structural biologists who study proteins, predicting their shape offers a key to understanding their function and accelerating treatments for diseases like cancer and COVID-19. The current approaches to accurately mapping that shape have their limitations, but by applying powerful machine learning methods to the large library of protein structures it is now possible to predict a protein’s shape from its gene sequence.
In a study appearing in Nature Plants, researchers from UC Davis, UC Berkeley, and Berkeley Lab report the discovery and characterization of a previously undescribed lineage of form I rubisco – one that the researchers suspect diverged from form I rubisco prior to the evolution of cyanobacteria. The novel lineage, called form I’ rubisco, gives researchers new insights into the structural evolution of form I rubisco, potentially providing clues as to how this enzyme changed the planet.
The work was led by Patrick Shih, a UC Davis assistant professor and the director of Plant Biosystems Design at the Joint BioEnergy Institute (JBEI), and Doug Banda, a postdoctoral scholar in his lab.
Lysine is an important amino acid that must be supplied in our diets, as our bodies can’t produce lysine on their own. Most cereal grains have low levels of lysine, and scientists have worked to breed crops with higher lysine levels.
However, the biochemical processes that break down lysine in plants weren’t fully understood. New Joint BioEnergy Institute (JBEI) research, published in Nature Communications, reveals this last missing step of lysine catabolism.
X-ray crystallography has been the most successful technique used to solve macromolecular structures, contributing several thousand new entries to the Protein Data Bank (PDB) every year. The protein crystal is the critical starting point for X-ray data collection, and consequently, its properties are correlated with the quality of the data and the level of detail that can be extracted for a macromolecular structure. However, proteins require solutions of specific composition to form crystals for structure determination studies. These specifications are usually determined from exposing the protein to several different solutions in a crystallization screen.
A team of researchers in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division led by Paul Adams and Jose Henrique Pereira have developed a new crystal screen, the Berkeley Screen, with 96 conditions proven to be highly effective at producing crystals for structural determination. The Berkeley Screen is now available to the wider crystallography community commercially.