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 Antibiotic effective against drug-resistant bacteria in pediatric skin infections
17.02.2017 | University of California - San Diego

nachricht Tiny magnetic implant offers new drug delivery method
14.02.2017 | University of British Columbia

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: Breakthrough with a chain of gold atoms

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

Im Focus: DNA repair: a new letter in the cell alphabet

Results reveal how discoveries may be hidden in scientific “blind spots”

Cells need to repair damaged DNA in our genes to prevent the development of cancer and other diseases. Our cells therefore activate and send “repair-proteins”...

Im Focus: Dresdner scientists print tomorrow’s world

The Fraunhofer IWS Dresden and Technische Universität Dresden inaugurated their jointly operated Center for Additive Manufacturing Dresden (AMCD) with a festive ceremony on February 7, 2017. Scientists from various disciplines perform research on materials, additive manufacturing processes and innovative technologies, which build up components in a layer by layer process. This technology opens up new horizons for component design and combinations of functions. For example during fabrication, electrical conductors and sensors are already able to be additively manufactured into components. They provide information about stress conditions of a product during operation.

The 3D-printing technology, or additive manufacturing as it is often called, has long made the step out of scientific research laboratories into industrial...

Im Focus: Mimicking nature's cellular architectures via 3-D printing

Research offers new level of control over the structure of 3-D printed materials

Nature does amazing things with limited design materials. Grass, for example, can support its own weight, resist strong wind loads, and recover after being...

Im Focus: Three Magnetic States for Each Hole

Nanometer-scale magnetic perforated grids could create new possibilities for computing. Together with international colleagues, scientists from the Helmholtz Zentrum Dresden-Rossendorf (HZDR) have shown how a cobalt grid can be reliably programmed at room temperature. In addition they discovered that for every hole ("antidot") three magnetic states can be configured. The results have been published in the journal "Scientific Reports".

Physicist Dr. Rantej Bali from the HZDR, together with scientists from Singapore and Australia, designed a special grid structure in a thin layer of cobalt in...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Booth and panel discussion – The Lindau Nobel Laureate Meetings at the AAAS 2017 Annual Meeting

13.02.2017 | Event News

Complex Loading versus Hidden Reserves

10.02.2017 | Event News

International Conference on Crystal Growth in Freiburg

09.02.2017 | Event News

 
Latest News

Biocompatible 3-D tracking system has potential to improve robot-assisted surgery

17.02.2017 | Medical Engineering

Real-time MRI analysis powered by supercomputers

17.02.2017 | Medical Engineering

Antibiotic effective against drug-resistant bacteria in pediatric skin infections

17.02.2017 | Health and Medicine

VideoLinks
B2B-VideoLinks
More VideoLinks >>>