3D Protein Imaging

Group I introns are a class of RNA elements that share a secondary structure which allows the intron to undergo self-splicing from the primary transcript. While most group I introns are located in the genes of mitochondria and chloroplasts of lower eucaryotes, some are found in nuclear genes. Interestingly, nuclear group I introns reside only in rDNA, the gene encoding rRNA, and when present they occupy all of the ca. 200 rDNA copies typical of eucaryotic organisms. Some group I introns are mobile genetic elements. They encode a site-specific endonuclease that recognizes and cleaves a DNA sequence at or near the intron insertion site of the intron-lacking allele. Among the ca. 150 nuclear group I introns reported so far, only three have been shown or have been inferred to be mobile: DiSSU1 from the slime mold Didymium iridis, NaSSU1 from the protist Naegleria andersoni and other Naegleria species, and PpLSU3 from the slime mold Physarum polycephalum. Originally found in the large-subunit rDNA gene of the Carolina strain (29), PpLSU3 contains the open reading frame (ORF) for the homing endonuclease I-PpoI. Here you can see the crystal structure of the I-Ppol endonuclease in complex to a synthetic target DNA, and isolated from Physarum polycephalum (PDB code: 8VNU) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dgDkAR-9 #molecularart #endonuclease #intron #crystal #xray #mobile

Transposable elements are DNA segments capable of moving between different locations1. They are widespread across all domains of life and have significantly affected genome diversity and evolution. Transposable elements can modulate gene expression, disseminate virulence and antibiotic resistance cassettes and are associated with numerous diseases. Several transposases rely on transposon-encoded regulators, including molecular matchmakers such as those found in Tn7, bacteriophage Mu and CRISPR RNA-guided elements, which belong to the ATPases associated with various cellular activities (AAA+) family of ATPases. The smallest and most abundant type of DNA transposons only contains proteins implicated in the transposition reaction. In bacteria, these are termed insertion sequences (ISs). The IS21 family is particularly widespread, has been found in clinically important multidrug-resistant strains and has shaped the evolution of human pathogens. Here you can see a cryoEM structure of the IstA-IstB strand transfer complex from Geobacillus stearothermophilus (PDB code: 8Q4D) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dZM4vxc9 #molecularart #transposon #transposase #complex #dna #mobile #cryoem

The A and B antigens of the ABO(H) blood group system are oligosaccharides present on the surface of human red blood cells that play a key role in determining compatibility of blood for transfusions. Blood group antigen epitopes are also present in mucin O-glycans in the intestinal mucosa. The blood group O antigen (H antigen) is composed of the trisaccharide Fuc-α1,2-Gal-β1,3-GlcNAc. The A and B antigens differ from H antigen by the addition of an extra sugar moiety, this being α1,3-linked GalNAc for A-type and Gal for B-type, to the β1,3-linked Gal residue. Because type O blood can theoretically be injected into patients with any of the ABO blood types, it is often considered a universal donor blood type. Attempts are being made to convert A and B antigens to the H antigen by hydrolyzing the GalNAc-α1,3- and Gal-α1,3-glycosidic linkages. The use of blood group converting enzymes, as exemplified by the recently discovered system using a combination of deacetylase and glycoside hydrolase (GH) family 36 α-galactosaminidase, is considered the most promising method for removing the desired sugars. Bifidobacteria are common inhabitants of the animal gastrointestinal tract. Infant gut-associated bifidobacteria, including Bifidobacterium bifidum, exert various beneficial effects on human health. B. bifidum assimilates mucin O-glycans and possesses many cell surface-anchored GHs that act on O-glycans. An α-galactosidase from B. bifidum JCM 1254 (AgaBb), which belongs to GH110 subfamily A and specifically acts on blood group B antigen, is an interesting tool to perform antigen transformations. Here you can see the crystal structure of blood group B alpha-1,3-galactosidase AgaBb from Bifidobacterium bifidum (PDB code: 8YK1) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dKwhd_ji #molecularart #blood #antigen #group #bifidobacterium #galactosidase #xray

🦠 𝗪𝗮𝗻𝘁 𝘁𝗼 𝗹𝗲𝗮𝗿𝗻 𝗵𝗼𝘄 𝘁𝗼 𝗱𝗿𝗮𝘄 𝘃𝗶𝗿𝘂𝘀𝗲𝘀 𝗮𝗻𝗱 𝗯𝗮𝗰𝘁𝗲𝗿𝗶𝗮 𝗮𝗰𝗰𝘂𝗿𝗮𝘁𝗲𝗹𝘆? 🎨🔬 Understanding the microscopic world is more important than ever, and what better way to communicate it than through 𝘀𝗰𝗶𝗲𝗻𝘁𝗶𝗳𝗶𝗰 𝗶𝗹𝗹𝘂𝘀𝘁𝗿𝗮𝘁𝗶𝗼𝗻? Whether you're a scientist, artist, or science communicator, our 𝗜𝗹𝘂𝘀𝘁𝗿𝗮 𝗠𝗶𝗰𝗿𝗼𝘀𝗰𝗼𝗽𝗶́𝗮 𝗖𝗼𝘂𝗿𝘀𝗲 ILLUSTRACIENCIA is back for its 𝟱𝘁𝗵 𝗲𝗱𝗶𝘁𝗶𝗼𝗻 and will equip you with the skills to visualize the invisible! 📌 𝗜𝗻 𝘁𝗵𝗶𝘀 𝗰𝗼𝘂𝗿𝘀𝗲, 𝘆𝗼𝘂 𝘄𝗶𝗹𝗹 𝗹𝗲𝗮𝗿𝗻 𝗵𝗼𝘄 𝘁𝗼: ✅ Illustrate 𝘃𝗶𝗿𝘂𝘀𝗲𝘀 and 𝗯𝗮𝗰𝘁𝗲𝗿𝗶𝗮 with scientific precision. ✅ 𝗦𝗲𝗮𝗿𝗰𝗵 𝘀𝗰𝗶𝗲𝗻𝘁𝗶𝗳𝗶𝗰 𝗱𝗮𝘁𝗮𝗯𝗮𝘀𝗲𝘀 for reliable references to ensure your illustrations are accurate. ✅ Design a 𝘀𝘁𝘂𝗻𝗻𝗶𝗻𝗴 𝘀𝗰𝗶𝗲𝗻𝘁𝗶𝗳𝗶𝗰 𝗺𝗮𝗴𝗮𝘇𝗶𝗻𝗲 𝗰𝗼𝘃𝗲𝗿 that captures attention while maintaining scientific integrity. 🖥️ For the final project, we’re collaborating with 3D Protein Imaging, using cutting-edge tools to visualize proteins in 3D. Plus, the final results will be shared through their networks, giving your work even more visibility! 🌐 Whether you're passionate about science, art, or both, this course will help you bridge the gap between scientific data and visual storytelling. 👉 𝗝𝗼𝗶𝗻 𝘂𝘀 𝘁𝗵𝗶𝘀 𝗝𝗮𝗻𝘂𝗮𝗿𝘆 𝗮𝗻𝗱 𝗯𝗿𝗶𝗻𝗴 𝘁𝗵𝗲 𝗺𝗶𝗰𝗿𝗼𝘀𝗰𝗼𝗽𝗶𝗰 𝘄𝗼𝗿𝗹𝗱 𝘁𝗼 𝗹𝗶𝗳𝗲! 𝗠𝗼𝗿𝗲 𝗶𝗻𝗳𝗼 & 𝘀𝗶𝗴𝗻 𝘂𝗽 𝗵𝗲𝗿𝗲 https://lnkd.in/dqBEuNp Let’s make science visible and beautiful! 🔬🎨 Visit more course projects: https://lnkd.in/dzPz_Nx9 #𝗦𝗰𝗶𝗲𝗻𝘁𝗶𝗳𝗶𝗰𝗜𝗹𝗹𝘂𝘀𝘁𝗿𝗮𝘁𝗶𝗼𝗻 #𝗠𝗶𝗰𝗿𝗼𝘀𝗰𝗼𝗽𝘆 #𝗦𝗰𝗶𝗲𝗻𝗰𝗲𝗖𝗼𝗺𝗺𝘂𝗻𝗶𝗰𝗮𝘁𝗶𝗼𝗻 #𝗩𝗶𝗿𝘂𝘀𝗔𝗿𝘁 #𝗕𝗮𝗰𝘁𝗲𝗿𝗶𝗮𝗜𝗹𝗹𝘂𝘀𝘁𝗿𝗮𝘁𝗶𝗼𝗻 #𝗗𝗮𝘁𝗮𝗩𝗶𝘀𝘂𝗮𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻 #𝟯𝗗𝗣𝗿𝗼𝘁𝗲𝗶𝗻𝗜𝗺𝗮𝗴𝗶𝗻𝗴 #𝗜𝗹𝗹𝘂𝘀𝘁𝗿𝗮𝗠𝗶𝗰𝗿𝗼𝘀𝗰𝗼𝗽𝗶𝗮 #𝗩𝗶𝘀𝘂𝗮𝗹𝗦𝘁𝗼𝗿𝘆𝘁𝗲𝗹𝗹𝗶𝗻𝗴 #𝗔𝗿𝘁𝗠𝗲𝗲𝘁𝘀𝗦𝗰𝗶𝗲𝗻𝗰𝗲 #𝟱𝘁𝗵𝗘𝗱𝗶𝘁𝗶𝗼𝗻

Nicotinic acetylcholine receptors, or nAChRs, are receptor polypeptides that respond to the neurotransmitter acetylcholine. Nicotinic receptors also respond to drugs such as the agonist nicotine. They are found in the central and peripheral nervous system, muscle, and many other tissues of many organisms. At the neuromuscular junction they are the primary receptor in muscle for motor nerve-muscle communication that controls muscle contraction. In the peripheral nervous system: (1) they transmit outgoing signals from the presynaptic to the postsynaptic cells within the sympathetic and parasympathetic nervous system, and (2) they are the receptors found on skeletal muscle that receive acetylcholine released to signal for muscular contraction. In the immune system, nAChRs regulate inflammatory processes and signal through distinct intracellular pathways. In insects, the cholinergic system is limited to the central nervous system. The nicotinic receptors are considered cholinergic receptors, since they respond to acetylcholine. Nicotinic receptors get their name from nicotine which does not stimulate the muscarinic acetylcholine receptors but selectively binds to the nicotinic receptors instead. The muscarinic acetylcholine receptor likewise gets its name from a chemical that selectively attaches to that receptor: muscarine. Acetylcholine itself binds to both muscarinic and nicotinic acetylcholine receptors. As ionotropic receptors, nAChRs are directly linked to ion channels. New evidence suggests that these receptors can also use second messengers (as metabotropic receptors do) in some cases. Nicotinic acetylcholine receptors are the best-studied of the ionotropic receptors. Here you can see a crystal structure of the acetylcholine binding receptor (AChBP) in complex with nicotine (PDB code: 1UW6) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dtJ_qjGw #molecularart #nicotine #receptor #acetylcholine #xray

Cystic fibrosis (CF) is a genetic disorder inherited in an autosomal recessive manner that impairs the normal clearance of mucus from the lungs, which facilitates the colonization and infection of the lungs by bacteria, notably Staphylococcus aureus. CF is a rare genetic disorder that affects mostly the lungs, but also the pancreas, liver, kidneys, and intestine. The hallmark feature of CF is the accumulation of thick mucus in different organs. Long-term issues include difficulty breathing and coughing up mucus as a result of frequent lung infections. Cystic fibrosis is inherited in an autosomal recessive manner. It is caused by the presence of mutations in both copies (alleles) of the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR) protein.Those with a single working copy are carriers and otherwise mostly healthy. CFTR is involved in the production of sweat, digestive fluids, and mucus. When the CFTR is not functional, secretions that are usually thin instead become thick. Here you can see the bottom-view of the cryoEM structure of human CFTR inserted into a membrane (PDB code: 5UAK) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dzuEwsi3 #molecularart #cystic #fibrosis #cftr #genetic #disease #mutation #mucus #infection #lung #cryoem

Borrelia burgdorferi is a bacterial species of the spirochete class in the genus Borrelia, and is one of the causative agents of Lyme disease in humans. Borrelia burgdorferi is a microaerophile, requiring small amounts of oxygen in order to undergo glycolysis and survive. Like all other Borrelia sps., this bacterium is also gram-negative and a spirochete. Borrelia colonies are often smaller, rounded, and white with an elevated center. B. burgdorferi circulates between Ixodes ticks and a vertebrate host in an enzootic cycle. B. burgdorferi living in a tick is mainly acquired through blood meals from an infected, competent vertebrate host. Ticks can transmit B. burgdorferi to humans, but humans are dead-end hosts, unlikely to continue the life cycle of the spirochete. Understanding the life cycle of this bacterium at the molecular level would help in finding new therapeutic options. Here you can see a cryoEM structure of the 50S ribosomal subunit in the Lyme disease pathogen Borrelia burgdorferi (PDB code: 8FN2) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dnhrHmMv #molecularart #lyme #borrelia #pathogen #ribosome #subunit #cryoem

A nucleosome is the basic repeating subunit of chromatin packaged inside the cell’s nucleus. In humans, about six feet of DNA must be packaged into a nucleus with a diameter less than a human hair, and nucleosomes play a key role in that process. A single nucleosome consists of about 150 base pairs of DNA sequence wrapped around a core of histone proteins. In forming a chromosome, the nucleosomes repeatedly fold in on themselves to tighten and condense the packaged DNA. Nucleosomes do a lot of things in our genomes. One of the most important is keeping chromosomes neatly organized and packed away. If you think about a tent that you might use to go camping, when you are storing it or carrying it from one place to another, it is tightly folded up so that it can fit in your backpack or on your bicycle. When it is time to use the tent, you unfold it and open it up so you have a shelter. Our DNA needs to be neatly folded up when it is in our cells so it doesn't get in the way when it isn't immediately being used, kind of like a folded tent. When our DNA is needed for something, maybe the cell needs to read the DNA or make a copy of it, a cell unfolds the DNA kind of like we'd unfold our tent. Nucleosomes are one of the main structures that help keep our DNA folded up neatly and packed away or help to unfold it. Here you can see a cryoEM structure of a plant nucleosome from Arabidopsis thaliana (PDB code: 8KCC) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dxTcZYyQ #molecularart #arabidopsis #plant #nucleosome #genome #structure #cryoem

Holliday junction (HJ) is a four-way structured DNA intermediate formed during the homologous recombination. At the end of the process, HJs must be resolved into two DNA duplexes that can be readily repaired by the DNA ligase. Successful HJ resolution requires two stepwise incisions across the junction center, which is catalyzed by a group of structure-selective DNA endonucleases, namely HJ resolvases. Based on the substrate specificity, HJ resolvases can be divided into two major categories: the canonical HJ resolvases, which includes RuvC, Hjc, Cce1 / Ydc2, GEN1and MOC; and the noncanonical HJ resolvases, such as SLX1-SLX4. Canonical HJ resolvases introduce two symmetrical nicks across the junction center by functioning as homodimers, and exhibit strong structure- and sequence-specificities in HJ cleavage.The RNase H-like enzymes, including RuvC and MOC1, typically feature three or more conserved carboxylates, known as the DDE motif, in their active sites. The catalysis of these enzymes is generally dependent on divalent cations, with a preference for Mg2+ and Mn2+. For the metal ion-assisted catalysis, a general two-metal-ion mechanism. Here you can see the crystal structure of the Zea mays MOC1 resolvase in complex with a nicked Holliday junction (PDB code: 8KFT) Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/d95-cAVJ #molecularart #dna #holiday #junction #resolvase #moc1 #xray

Burkholderia pseudomallei (Bps) is a soil-dwelling Gram-negative bacterium commonly found in Southeast Asia and Northern Australia and a cause of a deadly disease of mammalian species termed melioidosis. Patients infected with Bps usually develop skin ulcers, visceral abscesses, pneumonia and septicemia that imperatively require immediate antimicrobial treatment to avoid fatal progression of the disease. Very often, antimicrobial treatment is quite a challenge due to the high intrinsic broad spectrum resistance that most Bps strains exhibit towards a broad spectrum of antimicrobial agents including but not limited to β-lactam antibiotics, aminoglycosides, macrolides, and cephalosporins.Due to the high incidence of drug resistance and very high virulence, Bps is regarded a potential bioterrorism and warfare agent. As such, this organism has been listed by the US Centre for Disease Control and Prevention as a category B health hazard. Clinical and security concerns associated with Bps have justified intensive research in attempt to address the structural and functional organization of this pathogen as a prelude to the design of novel and efficacious anti-Bps therapeutic agents. Also known as porins, Omp channels are typical β-barrel protein structures that independently or as oligomeric units are inserted into the outer lipid bilayer of the bacterial cell wall to form pores through which extracellular species can diffuse and gain access to the periplasmic space and cytosol. In many cases, these porins are involved in the resistance against antibiotics. An Omp with an apparent molecular weight (MW) of 38 kDa, referred to as BpsOmp38, was isolated from the Bps cell wall. Here you can see the x-ray structure of the outer membrane porin BpsOmp38 of Burkholderia pseudomallei (PDB code: 8JTO). Rendering by Francisco J. Enguita (@paco.enguita) made with #ProteinImager https://lnkd.in/dwgPfwuv #molecularart #porin #resistance #outermembrane #antibiotic #Burkholderia #xray