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Scientists learn structure of enzyme in unusual virus

09-17-2007 · EurekAlert!

Biologists have determined the three-dimensional structure of an unusual viral enzyme that is required in the assembly of new viruses.

Keywords: scientists, learn, structure, enzyme, unusual, virus, scientist, viru

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Biologists learn structure of enzyme needed to power 'molecular motor'
03-22-2007 · EurekAlert!
Researchers at Purdue University and the Catholic University of America have discovered the structure of an enzyme essential for the operation of "molecular motors" that package DNA into the head segment of some viruses during their assembly.
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Scientists reveal DNA-enzyme interaction with first ever real time footage
09-17-2007 · EurekAlert!
For the first time scientists have been able to film, in real time, the nanoscale interaction of an enzyme and a DNA strand from an attacking virus. Researchers from the University of Cambridge have used a revolutionary Scanning Atomic Force Microscope in Japan to produce amazing footage of a protective enzyme unravelling the DNA of a virus trying to infect a bacterial host.
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Telomerase enzyme structure provides significant new target for anti-cancer therapies
11-13-2007 · EurekAlert!
Inappropriate activation of a single enzyme, telomerase, is associated with the uncontrollable proliferation of cells seen in as many as 90 percent of all of human cancers. Scientists have long eyed the enzyme as an ideal target for developing broadly effective anti-cancer drugs. Now, researchers working at the Wistar Institute have brought this goal closer by deciphering the 3-D structure of a domain, or region, of the telomerase molecule essential for the enzyme's activity.
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Advance in understanding of blood pressure gene could lead to new treatments
02-04-2007 · EurekAlert!
Research by scientists at UCL (University College London) has clearly demonstrated for the first time the structure and function of a gene crucial to the regulation of blood pressure. The discovery could be important in the search for new treatments for illnesses such as heart disease, the UK's biggest killer. In a paper published online today in Nature Medicine, the team, led by Professor Patrick Vallance and Dr James Leiper, UCL Department of Medicine, reveal the role of the human gene dimethylarginine dimethylaminohydrolase (DDAH), showing that loss of DDAH activity disrupts nitric oxide (NO) production. NO is critical in the regulation of blood pressure, nervous system functions and the immune system. The role of DDAH is to break down modified amino acids (Asymmetric dimethylarginine (ADMA) and monomethyl arginine (L-NMMA)) that are produced by the body and have been shown to inhibit NO synthase. These molecules accumulate in various disease states including diabetes, renal failure and pulmonary and systemic hypertension, and their concentration in plasma (the fluid component of blood) is strongly predicative of cardiovascular disease and death. In a healthy human body, the majority of ADMA is eliminated through active metabolism by DDAH. Scientists have hypothesised that if DDAH function is impaired, NO production is reduced, and that this could be an important feature of increased cardiovascular risk. To examine this pathway in more detail, the researchers deleted the DDAH gene in mice. These mice went on to develop hypertension, or high blood pressure. They also designed specific inhibitors (small molecules) which bind to the active site of human DDAH. These small molecule inhibitors also induced hypertension in mice, confirming the importance of DDAH in the regulation of blood pressure. Dr Leiper, UCL Medicine, said: “These genetic and chemical approaches to disrupt DDAH showed remarkably consistent results, and provide compelling evidence that loss of DDAH function increases the concentration of ADMA and thereby disrupts vascular NO signalling. “There has been considerable scientific interest in this pathway and the role of ADMA as a novel risk factor, but so far there's been little evidence to support the idea that it's a cause of disease, rather than just a marker. Genes and their pathways are crucial to our understanding of cardiovascular disease and a better understanding of DDAH-1 could lead to important new treatments. “It could help us to establish if genetic variation predisposes certain people to these diseases, or whether environmental factors exert some of their effects through modulation of DDAH activity. “Our research also shows that this pathway could be harnessed therapeutically to limit production of NO in certain situations where too much nitric oxide is a bad thing; for example, hypotension and septic shock. These are some of the biggest problems in intensive care medicine and there is a huge unmet need for drug treatments.” The study, which was carried out at UCL's Rayne Institute, was funded by grants from the British Heart Foundation, the Wellcome Trust and the Medical Research Council. Professor Jeremy Pearson, Associate Medical Director of the British Heart Foundation, said: "The unexpected finding in the 1980s that a simple gas, nitric oxide (NO), is made by cells in the blood vessel wall and is a powerful control of blood vessel relaxation led to the award of the Nobel Prize in 1998 to its discoverers. "More recently, there has been increasing evidence that impairment of NO production is likely to be an important factor in the development of heart and circulatory disease, but the mechanisms responsible are not fully understood. "This study suggests for the first time that the loss of the activity of the enzyme DDAH-1 leads to reduced NO production and may cause heart and circulatory disease. These findings are likely to be important in the search for new ways to optimise the health of our blood vessels." ### Notes for Editors 1. For more information, please contact Ruth Metcalfe in the UCL Media Relations Office on tel: +44 (0)20 7679 9739, mobile: +44 (0)7990 675 947, out of hours: +44 (0)7917 271 364, e-mail: r.metcalfe@ucl.ac.uk2. 'Disruption of methylarginine metabolism impairs vascular homeostasis' is published in the February issue of the journal Nature Medicine. Advance online publication is embargoed to 18.00 GMT (13.00 US Eastern) Sunday 4 February 2007. Journalists can obtain copies of the paper by contacting the UCL Media Relations Office.3. The study was funded by the British Heart Foundation, the Wellcome Trust and the Medical Research Council. About UCL Founded in 1826, UCL was the first English university established after Oxford and Cambridge, the first to admit students regardless of race, class, religion or gender, and the first to provide systematic teaching of law, architecture and medicine. In the government's most recent Research Assessment Exercise, 59 UCL departments achieved top ratings of 5* and 5, indicating research quality of international excellence. UCL is the fourth-ranked UK university in the 2006 league table of the top 500 world universities produced by the Shanghai Jiao Tong University. UCL alumni include Mahatma Gandhi (Laws 1889, Indian political and spiritual leader); Jonathan Dimbleby (Philosophy 1969, writer and television presenter); Junichiro Koizumi (Economics 1969, Prime Minister of Japan); Lord Woolf (Laws 1954, Lord Chief Justice of England & Wales); Alexander Graham Bell (Phonetics 1860s, inventor of the telephone), and members of the band Coldplay.
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Study holds promise for new way to fight AIDS
11-01-2006 · EurekAlert!
For years researchers have been trying to understand how a few HIV-infected patients naturally defeat a virus that otherwise overwhelms the immune system. New information about the structure of a key enzyme represents an early step toward the design of a new class of drugs that could afford to all the same natural protection enjoyed by few.
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Protein averts cell suicide but might contribute to cancer
03-29-2007 · EurekAlert!
Scientists have discovered how an unusual protein helps a cell bypass damage when making new DNA, thereby averting the cell's self-destruction. But they also discovered that this protein, an enzyme called Dpo4, often makes errors when copying the genomic DNA sequence that later might cause the cell to become cancerous.
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Translating form into function
07-01-2007 · EurekAlert!
In the last 40 years, scientists have perfected ways to determine the knot-like structure of enzymes, but they've been stumped trying to translate the structure into an understanding of function -- what the enzyme actually does in the body. This puzzle has hurt drug discovery, since many of the most successful drugs work by blocking enzyme action. Now, in an expedited article in Nature, researchers show that a solution to the puzzle is finally in sight.
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Brown scientists map structure of DNA-doctoring protein complex
12-06-2006 · EurekAlert!
Mobile DNA, which inserts foreign genes into target cells, is a powerful force in the march of evolution and the spread of disease. Working with the lambda virus and E. coli bacteria, Brown University biologists have solved the structure of a six-protein complex critical to performing this gene-grafting surgery. The technique they developed could be used to reveal the structure of other critical protein complexes, landing the work on the cover of Molecular Cell.
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Changes in amino acids in the 1918 influenza virus cut transmission
02-01-2007 · EurekAlert!
Modest changes in the 1918 flu virus's hemagglutinin receptor binding site -- a molecular structure critical for the spread of infection -- stopped viral transmission in ferrets, according to a new study conducted by researchers at Mount Sinai School of Medicine and at the Centers for Disease Control and Prevention. The finding, published in the February 1 issue of Science, could have significant clinical implications in helping scientists develop ways to break the disease cycle and possibly help reduce the risk for a potential pandemic.
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Invisible for electrons
03-06-2007 · EurekAlert!
As thin as it gets: the carbon membranes recently created by Max Planck scientists are only one atom thick. For electrons, such membranes are almost completely transparent -- using an electron microscope, scientists may thus be able to examine absorbed individual molecules on the membranes, and image the atomic structure of complex biological molecules. Such ultra-thin membranes may also be used to filter out gases (Nature, March 1, 2007).
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