Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

’Knot’ to be undone, researchers discover unusual protein structure

27.11.2002


Researchers funded by the National Institute of General Medical Sciences have determined the structure of a protein with a surprising feature in it: a knot. This is the first time a knot has been found in a protein from the most ancient type of single-celled organism, an archaebacterium, and one of only a few times a knot has been seen in any protein structure.



This very unusual protein shape finding is a result from the NIGMS Protein Structure Initiative, a 10-year effort to determine 10,000 unique protein structures using fast, highly automated methods. NIGMS, a component of the U.S. Department of Health and Human Services’ National Institutes of Health, provides $50 million per year to nine PSI research centers. The protein knot structure was solved at one of the PSI centers, the Midwest Center for Structural Genomics, which is directed by Andrzej Joachimiak, Ph.D., of Argonne National Laboratory in suburban Chicago.

The researchers describe the new protein structure in the journal Proteins. Their article will be published online Nov. 27 and in print in early December.


"It’s a surprising and different structure," said NIGMS’ John Norvell, Ph.D., director of the Protein Structure Initiative. Protein folding theory previously held that forming a knot was beyond the ability of a protein. Joachimiak suggests that the newly discovered knot may stabilize the amino acid subunits of the protein.

Such discoveries are just what the PSI aims for. "The PSI approach is to solve thousands of unique protein structures," said Norvell. "It’s a discovery-driven effort, a voyage into the unknown. We aren’t sure what we’ll find, but we expect to map a great diversity of protein structures."

"This makes us want to find out why nature goes to the trouble of creating a knot instead of a more typical fold," said Joachimiak.

One of the main goals of the PSI is to understand all of the possible shapes of proteins in nature. Scientists hope that understanding the full range of protein shapes will shed light on the mysterious process proteins use to fold into a three-dimensional structure from a linear chain of amino acid subunits. Ideally, scientists would like to be able to predict the shape of a protein from the sequence of the gene that codes for it. This ability could be immensely useful in understanding diseases and developing new drugs because a protein’s shape offers big clues to its function and can point to ways of controlling that function.

The "high-throughput" PSI approach is radically different from how scientists have approached protein structure determination in the past. Until recently, scientists focused on solving the structures of proteins with known functions.

The newly discovered knotted protein comes from a microorganism called Methanobacterium thermoautotrophicum. This organism is of interest to industry for its ability to break down waste products and produce methane gas. Scientists know which gene codes for the 268-amino acid protein, but they do not know the protein’s function. They speculate that it binds to RNA, a chemical cousin of the genetic material DNA, and helps process this molecule.

The PSI, currently in its pilot phase, expects to move into production phase by the end of 2005. By the end of the pilot phase, each center will aim to produce 100 to 200 new protein structures per year, adding greatly to the number of known structures. The PSI also expects to dramatically lower the average cost of solving a structure.

The paper describing the new structure was authored by scientists at Argonne National Laboratory and the University of Toronto. The nation’s first national laboratory, Argonne conducts basic and applied scientific research across a wide spectrum of disciplines, ranging from high-energy physics to climatology and biotechnology. The laboratory is operated by the University of Chicago as part of the U.S. Department of Energy’s national laboratory system.


NIGMS supports basic biomedical research and training nationwide. NIGMS-funded studies lay the foundation for advances in disease diagnosis, treatment and prevention. To learn more, visit the NIGMS Web site at www.nigms.nih.gov.

For information about the protein knot, contact Linda Joy in the NIGMS Office of Communications and Public Liaison at 301-496-7301 to speak with PSI director John Norvell, Ph.D, or Catherine Foster of Argonne National Laboratory at 630-252-5580 to speak with Andrzej Joachimiak, Ph.D.

REFERENCE

Zarembinski TI, Kim Y, Peterson K, Christendat D, Kharamsi A, Arrowsmith CH, Edwards AM, Joachimiak A. Deep trefoil knot implicated in RNA binding found in an archaebacterial protein. Proteins 2002; 50: 177-183.


Linda Joy | EurekAlert!
Further information:
http://www.nih.gov/nigms

More articles from Health and Medicine:

nachricht Scientists find new approach that shows promise for treating cystic fibrosis
14.03.2019 | NIH/National Heart, Lung and Blood Institute

nachricht Lab grown ‘brains’ successfully model disease
13.03.2019 | Max-Planck-Institut für Psychiatrie

All articles from Health and Medicine >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Revealing the secret of the vacuum for the first time

New research group at the University of Jena combines theory and experiment to demonstrate for the first time certain physical processes in a quantum vacuum

For most people, a vacuum is an empty space. Quantum physics, on the other hand, assumes that even in this lowest-energy state, particles and antiparticles...

Im Focus: Sussex scientists one step closer to a clock that could replace GPS and Galileo

Physicists in the EPic Lab at University of Sussex make crucial development in global race to develop a portable atomic clock

Scientists in the Emergent Photonics Lab (EPic Lab) at the University of Sussex have made a breakthrough to a crucial element of an atomic clock - devices...

Im Focus: Sensing shakes

A new way to sense earthquakes could help improve early warning systems

Every year earthquakes worldwide claim hundreds or even thousands of lives. Forewarning allows people to head for safety and a matter of seconds could spell...

Im Focus: A thermo-sensor for magnetic bits

New concept for energy-efficient data processing technology

Scientists of the Department of Physics at the University of Hamburg, Germany, detected the magnetic states of atoms on a surface using only heat. The...

Im Focus: The moiré patterns of three layers change the electronic properties of graphene

Combining an atomically thin graphene and a boron nitride layer at a slightly rotated angle changes their electrical properties. Physicists at the University of Basel have now shown for the first time the combination with a third layer can result in new material properties also in a three-layer sandwich of carbon and boron nitride. This significantly increases the number of potential synthetic materials, report the researchers in the scientific journal Nano Letters.

Last year, researchers in the US caused a big stir when they showed that rotating two stacked graphene layers by a “magical” angle of 1.1 degrees turns...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

VideoLinks
Industry & Economy
Event News

International Modelica Conference with 330 visitors from 21 countries at OTH Regensburg

11.03.2019 | Event News

Selection Completed: 580 Young Scientists from 88 Countries at the Lindau Nobel Laureate Meeting

01.03.2019 | Event News

LightMAT 2019 – 3rd International Conference on Light Materials – Science and Technology

28.02.2019 | Event News

 
Latest News

Researchers measure near-perfect performance in low-cost semiconductors

18.03.2019 | Power and Electrical Engineering

Nanocrystal 'factory' could revolutionize quantum dot manufacturing

18.03.2019 | Materials Sciences

Long-distance quantum information exchange -- success at the nanoscale

18.03.2019 | Physics and Astronomy

VideoLinks
Science & Research
Overview of more VideoLinks >>>