A set of genes from a marine bacterium has been found to encode the biosynthesis of a promising antidepressant drug candidate. This work, which used the ALS to solve the structure of a key enzyme, could enable industrial-scale bioproduction of the drug in ways that are more efficient and sustainable than chemical synthesis. Read more »
A Citizen-Science Computer Game for Protein Design
Using the computer game, “Foldit,” nonexpert citizen scientists designed new proteins whose structures, verified at the ALS, were equivalent in quality to and more structurally diverse than computer-generated designs. The work shows the potential of using crowd-based creativity in the design of new proteins for fighting illness and disease. Read more »
Locking Protein Structure to Close the Door on Cancer
While the SHP2 protein helps regulate cellular activity, mutations in its structure can lead to cancer. X-ray crystallography at the ALS and SSRL has revealed differences between normal and mutated SHP2, as well as how it binds to certain cancer drugs. These structural insights open the door to new types of cancer therapy. Read more »
Structure Reveals Mechanism Behind Periodic Paralysis
X-ray crystallography of a membrane protein provided a structural understanding of how a single mutation can result in periodic muscle paralysis. The results suggest possible drug designs that could provide relief to patients with a genetic disorder that causes them to be overcome suddenly with profound muscle weakness. Read more »
NIH Grant Will Enhance Structural Biology Research Experience for ALS Users
A recently awarded National Institutes of Health (NIH) grant will help integrate existing structural biology resources at the ALS to better serve users. The funds will help establish a centralized collaborative mechanism, called ALS-ENABLE, that will guide users through the most appropriate routes for answering their biological questions. Read more »
Exploring the Roots of Photosynthesis in a Soil-Dwelling Bacterium
The bacterium, H. modesticaldum, is thought to have a photosynthetic reaction center resembling the earliest common ancestor of all photosynthesis complexes. Its molecular structure has now been solved, providing insight into the evolution of photosynthesis and how nature optimized light-driven energy collection. Read more »
Bending the (β-Sheet) Curve to Shape Protein Cavities
Curved β sheets are basic building blocks of many protein cavities that, by serving as binding sites for other molecules, are essential to protein function. β-sheet curvature can now be controlled with atomic-level accuracy, opening the door to custom-designed sites capable of entirely new functions. Read more »
NCAA Drives Formation of Designed Proteins
A noncanonical amino-acid (NCAA) complex has been found to drive the self-assembly of a computationally designed protein. Bpy-ala, which is “noncanonical” because it’s not among the 20 amino acids that occur naturally, has useful properties that could be used to generate novel photoactive proteins. Read more »
Two Basic Mechanisms of Cardiovascular Drugs
The structures of proteins controlling calcium-ion transport through cell membranes have been revealed, bound to two drugs known as calcium channel blockers. The discovery might accelerate the development of safer and more effective drugs for treating cardiovascular disorders such as high blood pressure, chest pain, and irregular heartbeat. Read more »
Validation of Novel Proteins Inspired by Nature
Designed proteins containing hydrogen-bonding modules have been validated by crystallography and SAXS. The ability to design synthetic molecules that combine the specificity of DNA-like binding with protein function opens up huge opportunities for the fields of synthetic biology and materials science. Read more »
