'Invisible' protein structure explains the power of enzymes

July 03, 2015

A research group at Umeå University in Sweden has managed to capture and describe a protein structure that, until now, has been impossible to study. The discovery lays the base for developing designed enzymes as catalysts to new chemical reactions for instance in biotechnological applications. The result of the study is published in the journal Nature Communications.

Enzymes are extraordinary biocatalysts able to speed up the cellular, chemical reactions several million times. This increase of speed is completely necessary for all biological life, which would otherwise be limited by the slow nature of vital chemical reactions. Now, a research group at the Department of Chemistry has discovered a new aspect in enzymes that, in part, explains how enzymes manage their tasks with unmatched efficiency and selectivity.

So-called high-energy states in enzymes are regarded as necessary for catalysing of chemical reactions. A high-energy level is a protein structure only occurring temporarily and for a short period of time; and these factors collaborate until its state becomes invisible to traditional spectroscopic techniques. The Umeå researchers have managed to find a way to maintain a high-energy state in the enzyme, adenylate kinase, by mutating the protein.

"Thanks to this enrichment, we have been able to study both structure and dynamics of this state. The study shows that enzymatic high-energy states are necessary for chemical catalysis," says Magnus Wolf-Watz, research group leader at the Department of Chemistry.

The study also indicates a possibility to fine-tune the dynamics of an enzyme and this possibility can be useful for researchers in developing new enzymes for catalysis of new chemical reactions.

"Research on Bioenergy is an active field at Umeå University. An important, practical application of the new knowledge can be enzymatic digestion of useful molecules from wooden raw materials," says Magnus Wolf-Watz.

The discovery has been made possible thanks to a broad scientific approach where numerous advanced biophysical techniques have been used; Nuclear Magnetic Resonance (NMR) and x-ray crystallography being the main techniques.

"One of the strengths of Umeå University is the open cooperative climate with low or no barriers between research groups. It means that exciting research can be conducted in the borderland of differing expertise," says Magnus Wolf-Watz.
-end-
The main author of the article is Michael Kovermann who has completed his postdoctoral position at Umeå University and will shortly return to Germany for a professorship at the University of Konstanz.

About NMR for Life:

Based on major funding by Wallenberg and Kempe foundations, the NMR platform at Umeå University has access to instruments in world class. The instrumentation is a national NMR infrastructure operated in collaboration with the University of Gothenburg and is accessible to the Swedish academic and industrial research community. Umeå University platform managers are Professor Gerhard Gröbner and Professor Jürgen Schleucher.

http://www.nmrforlife.se/

Published article:

Michael Kovermann, Jörgen Ådén, Christin Grundström, A. Elisabeth Sauer-Eriksson, Uwe H. Sauer & Magnus Wolf-Watz: Structural basis for catalytically restrictive dynamics of a high-energy enzyme state. Nature Communications. DOI: 10.1038/ncomms8644.

http://www.nature.com/naturecommunications

Umea University

Related Protein Articles from Brightsurf:

The protein dress of a neuron
New method marks proteins and reveals the receptors in which neurons are dressed

Memory protein
When UC Santa Barbara materials scientist Omar Saleh and graduate student Ian Morgan sought to understand the mechanical behaviors of disordered proteins in the lab, they expected that after being stretched, one particular model protein would snap back instantaneously, like a rubber band.

Diets high in protein, particularly plant protein, linked to lower risk of death
Diets high in protein, particularly plant protein, are associated with a lower risk of death from any cause, finds an analysis of the latest evidence published by The BMJ today.

A new understanding of protein movement
A team of UD engineers has uncovered the role of surface diffusion in protein transport, which could aid biopharmaceutical processing.

A new biotinylation enzyme for analyzing protein-protein interactions
Proteins play roles by interacting with various other proteins. Therefore, interaction analysis is an indispensable technique for studying the function of proteins.

Substituting the next-best protein
Children born with Duchenne muscular dystrophy have a mutation in the X-chromosome gene that would normally code for dystrophin, a protein that provides structural integrity to skeletal muscles.

A direct protein-to-protein binding couples cell survival to cell proliferation
The regulators of apoptosis watch over cell replication and the decision to enter the cell cycle.

A protein that controls inflammation
A study by the research team of Prof. Geert van Loo (VIB-UGent Center for Inflammation Research) has unraveled a critical molecular mechanism behind autoimmune and inflammatory diseases such as rheumatoid arthritis, Crohn's disease, and psoriasis.

Resurrecting ancient protein partners reveals origin of protein regulation
After reconstructing the ancient forms of two cellular proteins, scientists discovered the earliest known instance of a complex form of protein regulation.

Sensing protein wellbeing
The folding state of the proteins in live cells often reflect the cell's general health.

Read More: Protein News and Protein Current Events
Brightsurf.com is a participant in the Amazon Services LLC Associates Program, an affiliate advertising program designed to provide a means for sites to earn advertising fees by advertising and linking to Amazon.com.