Scientists recently discovered the full molecular structure of telomerase, an enzyme important to aging and cancer. Within each cell, telomerase maintains the telomeres, or end pieces, of a chromosome, preserving genetic data and extending the life of the cell. In their study, a team from UCLA and UC Berkeley found the subunit p50, shown in red, to be a keystone in the enzyme's structure and function. Featured in the May 16, 2013 issue of Biomedical Beat.

Cell showing overproduction of the ARTS protein (red). ARTS triggers apoptosis, as shown by the activation of caspase-3 (green) a key tool in the cell's destruction. The nucleus is shown in blue. Image is featured in October 2015 Biomedical Beat blog post Cool Images: A Halloween-Inspired Cell Collection.

Just as our bodies rely on bones for structural support, our cells rely on a cellular skeleton. In addition to helping cells keep their shape, this cytoskeleton transports material within cells and coordinates cell division. One component of the cytoskeleton is a protein called tubulin, shown here as thin strands.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

The enzyme CCP is found in the mitochondria of baker’s yeast. Scientists study the chemical reactions that CCP triggers, which involve a water molecule, iron, and oxygen. This structure was determined using an X-ray free electron laser.

Model of the mandelate racemase enzyme from Bacillus subtilis, a bacterium commonly found in soil.

Crystals of porcine trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

A global "map of the protein structure universe." The Berkeley Structural Genomics Center has developed a method to visualize the vast universe of protein structures in which proteins of similar structure are located close together and those of different structures far away in the space. This map, constructed using about 500 of the most common protein folds, reveals a highly non-uniform distribution, and shows segregation between four elongated regions corresponding to four different protein classes (shown in four different colors). Such a representation reveals a high-level of organization of the protein structure universe.

The proteasome is a critical multiprotein complex in the cell that breaks down and recycles proteins that have become damaged or are no longer needed. This movie shows how a protein substrate (red) is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region then gets engaged by the AAA+ motor of the proteasome (cyan), which initiates mechanical pulling, unfolding and movement of the protein into the proteasome's interior for cleavage into shorter protein pieces called peptides. During movement of the substrate, its ubiquitin modification gets cleaved off by the deubiquitinase Rpn11 (green), which sits directly above the entrance to the AAA+ motor pore and acts as a gatekeeper to ensure efficient ubiquitin removal, a prerequisite for fast protein breakdown by the 26S proteasome. Related to image 3763.

Crystals of fungal lipase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

These images model the molecular structures of three enzymes with critical roles in the life cycle of the human immunodeficiency virus (HIV). At the top, reverse transcriptase (orange) creates a DNA copy (yellow) of the virus's RNA genome (blue). In the middle image, integrase (magenta) inserts this DNA copy in the DNA genome (green) of the infected cell. At the bottom, much later in the viral life cycle, protease (turquoise) chops up a chain of HIV structural protein (purple) to generate the building blocks for making new viruses. See these enzymes in action on PDB 101’s video A Molecular View of HIV Therapy.

Enzymes speed up chemical reactions by reducing the amount of energy needed for the reactions. The substrate (lactose) binds to the active site of the enzyme (lactase) and is converted into products (sugars).

This illustration highlights spherical pre-synaptic vesicles that carry the neurotransmitter glutamate. The presynaptic and postsynaptic membranes are shown with proteins relevant for transmitting and modulating the neuronal signal.

PDB 101’s Opioids and Pain Signaling video explains how glutamatergic synapses are involved in the process of pain signaling.

This image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. By helping to link the amino acid tryptophan to a tRNA molecule, TrpRS primes the amino acid for use in protein synthesis. A cluster of iron and sulfur atoms (orange and red spheres) was unexpectedly found in the anti-codon domain, a key part of the molecule, and appears to be critical for the function of the enzyme. TrpRS was discovered in Thermotoga maritima, a rod-shaped bacterium that flourishes in high temperatures.

A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

Model of a member from the Tex protein family, which is implicated in transcriptional regulation and highly conserved in eukaryotes and prokaryotes. The structure shows significant homology to a human transcription elongation factor that may regulate multiple steps in mRNA synthesis.

A zebrafish embryo showing its natural colors. Zebrafish have see-through eggs and embryos, making them ideal research organisms for studying the earliest stages of development. This image was taken in transmitted light under a polychromatic polarizing microscope.

X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3417, and 3419.

This image shows how the CRISPR surveillance complex is disabled by two copies of anti-CRISPR protein AcrF1 (red) and one AcrF2 (light green). These anti-CRISPRs block access to the CRISPR RNA (green tube) preventing the surveillance complex from scanning and targeting invading viral DNA for destruction.